@misc{fox1963abiotic6,
    author = "Fox, S. W. and Yuyama, S",
    title = "Abiotic production of primitive protein and formed microparticles",
    year = "1963",
    howpublished = "Annals of the New York Academy of Sciences, v. 108, p. 487-494",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., and Yuyama, S., 1963, Abiotic production of primitive protein and formed microparticles: Annals of the New York Academy of Sciences, v. 108, p. 487-494.}"
}

@article{fox1963effects5,
    author = "Fox, S. W. and Yuyama, S",
    title = "Effects of the Gram stain on microspheres from thermal polyamino acids",
    year = "1963",
    journal = "Journal of Bacteriology, v. 85, p. 279-283",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., and Yuyama, S., 1963, Effects of the Gram stain on microspheres from thermal polyamino acids: Journal of Bacteriology, v. 85, p. 279-283.}"
}

@article{doi1010160303264771900037,
    author = "Hsu, Laura and Brooke, Steven and Fox, Sidney W.",
    title = "Conjugation of proteinoid microspheres: A model of primordial communication",
    year = "1971",
    journal = "Biosystems",
    url = "https://doi.org/10.1016/0303-2647(71)90003-7",
    doi = "10.1016/0303-2647(71)90003-7",
    openalex = "W2135541201",
    references = "doi101002bbpc19080141703, doi101007bf00599584, doi1010160010406x67900515, doi1010160012160667900504, doi1010160014482761903470, doi101021ja01499a069, doi101073pnas6041092, doi101073pnas622399, doi101093aibsbulletin3215c, doi101126science1703961984"
}

@misc{hsu1971conjugation7,
    author = "Hsu, L. L. and Brooke, S. and Fox, S. W",
    title = "Conjugation of proteinoid microspheres",
    year = "1971",
    howpublished = "a model of primordial communication: Current Models in Biology [Now BioSystems], v. 4, p. 12-25",
    note = "talkorigins\_source = {true}; raw\_reference = {Hsu, L. L., Brooke, S., and Fox, S. W., 1971, Conjugation of proteinoid microspheres: a model of primordial communication: Current Models in Biology [Now BioSystems], v. 4, p. 12-25.}"
}

@misc{mueller1972organic10,
    author = "Mueller, G",
    title = "Organic microspheres from the Precambrian of South-West Africa",
    year = "1972",
    howpublished = "Nature, v. 235, p. 90-95",
    note = "talkorigins\_source = {true}; raw\_reference = {Mueller, G., 1972, Organic microspheres from the Precambrian of South-West Africa: Nature, v. 235, p. 90-95.}"
}

@article{doi101007bf00623555,
    author = "Jungck, John R. and Fox, Sidney W.",
    title = "Synthesis of oligonucleotides by proteinoid microspheres acting on ATP",
    year = "1973",
    journal = "Die Naturwissenschaften",
    url = "https://doi.org/10.1007/bf00623555",
    doi = "10.1007/bf00623555",
    openalex = "W2090234738",
    references = "doi101007bf00602509, doi101007bf00623322, doi1010160016003256901545, doi1010160022283668903926, doi1010160026265x73901124, doi101016s0047248478800529, doi101073pnas505905, doi101126science147365368, doi101126science1734000875, doi104159harvard9780674188693"
}

@article{doi1010160303264773900026,
    author = "Ryan, Jack Woodrow and Fox, Sidney W.",
    title = "Activation of glycine by ATP, a divalent cation, and proteinoid microspheres",
    year = "1973",
    journal = "Biosystems",
    url = "https://doi.org/10.1016/0303-2647(73)90002-6",
    doi = "10.1016/0303-2647(73)90002-6",
    openalex = "W2035399108"
}

@techreport{easton1973a1,
    author = "Easton, T. A",
    title = "A note on the mathematics of microsphere division",
    year = "1973",
    howpublished = "Bulletin of Mathematical Biology, v. 35, p. 259-262",
    note = "talkorigins\_source = {true}; raw\_reference = {Easton, T. A., 1973, A note on the mathematics of microsphere division: Bulletin of Mathematical Biology, v. 35, p. 259-262.}"
}

@phdthesis{junck1973synthesis9,
    author = "Junck, J. R. and Fox, S. W",
    title = "Synthesis of oligonucleotides by proteinoid microspheres acting on ATP",
    year = "1973",
    publisher = "Naturwissenschaften, v. 60, p. 425-427",
    note = "talkorigins\_source = {true}; raw\_reference = {Junck, J. R., and Fox, S. W., 1973, Synthesis of oligonucleotides by proteinoid microspheres acting on ATP: Naturwissenschaften, v. 60, p. 425-427.}"
}

@article{doi101007978940102239219,
    author = "Fox, Sidney W. and Jungck, John R. and Nakashima, Tadayoshi",
    title = "From Proteinoid Microsphere to Contemporary Cell: Formation of Internucleotide and Peptide Bonds by Proteinoid Particles",
    year = "1974",
    url = "https://doi.org/10.1007/978-94-010-2239-2\_19",
    doi = "10.1007/978-94-010-2239-2\_19",
    openalex = "W1977729334",
    references = "doi101007bf00602509, doi101007bf01101286, doi1010160016003256901545, doi1010160026265x73901124, doi1010160303264771900037, doi101016s0047248478800529, doi101038scientificamerican085444, doi101073pnas5641325, doi101073pnas591110, doi101351pac197334030641"
}

@article{doi101007bf00927027,
    author = "Fox, Sidney W. and Jungck, John R. and Nakashima, Tadayoshi",
    title = "From proteinoid microsphere to contemporary cell: Formation of internucleotide and peptide bonds by proteinoid particles",
    year = "1974",
    journal = "Origins of Life and Evolution of Biospheres",
    url = "https://doi.org/10.1007/bf00927027",
    doi = "10.1007/bf00927027",
    openalex = "W4236817780",
    references = "doi101007bf00602509, doi101007bf00623555, doi1010160010406x67900515, doi1010160016003256901545, doi1010160026265x73901124, doi1010160303264773900026, doi101038scientificamerican085444, doi101073pnas5641325, doi101073pnas591110, doi1010970000044119591000000029, doi101351pac197334030641"
}

@misc{fox1974from4,
    author = "Fox, S. W. and Jungck, J. R. and Nakashima, T",
    title = "From proteinoid microsphere to comtemporary cell",
    year = "1974",
    howpublished = "formation of internucleotide and peptide bonds by proteinoid particles: Origins Life, v. 5, p. 227-237",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., Jungck, J. R., and Nakashima, T., 1974, From proteinoid microsphere to comtemporary cell: formation of internucleotide and peptide bonds by proteinoid particles: Origins Life, v. 5, p. 227-237.}"
}

@misc{fox1974the2,
    author = "Fox, S. W",
    title = "The proteinoid theory of the origin of life and competing ideas",
    year = "1974",
    howpublished = "American Biology Teacher, v. 36, p. 161-172, 181",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., 1974, The proteinoid theory of the origin of life and competing ideas: American Biology Teacher, v. 36, p. 161-172, 181.}"
}

@article{doi101007bf01372406,
    author = "Rohlfing, Duane L.",
    title = "Coacervate-like microspheres from lysine-rich proteinoid",
    year = "1975",
    journal = "Origins of Life and Evolution of Biospheres",
    url = "https://doi.org/10.1007/bf01372406",
    doi = "10.1007/bf01372406",
    openalex = "W2066069868",
    references = "rohlfing1969catalytic"
}

@article{doi1010160303264777900284,
    author = "Brooke, Steven and Fox, Sidney W.",
    title = "Compartmentalization in proteinoid microspheres",
    year = "1977",
    journal = "Biosystems",
    url = "https://doi.org/10.1016/0303-2647(77)90028-4",
    doi = "10.1016/0303-2647(77)90028-4",
    openalex = "W1992807593",
    references = "doi101007bf00623322, doi101007bf01372406, doi101007bf01659185, doi101007bf01732178, doi1010160026265x73901124, doi101016s0047248478800529, doi101111j155856461975tb00851x, doi101126science1473658563, doi105962bhltitle1018, openalexw2983085323"
}

@misc{fox1980metabolic3,
    author = "Fox, S. W",
    title = "Metabolic microspheres",
    year = "1980",
    howpublished = "Naturwissenschaften, v. 67, p. 378-383",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., 1980, Metabolic microspheres: Naturwissenschaften, v. 67, p. 378-383.}"
}

@misc{ishima1981electrical8,
    author = "Ishima, Y. and Pryzbylski, A. and Fox, S. W",
    title = "Electrical membrane phenomena in spherules from protenoid and lecithin",
    year = "1981",
    howpublished = "BioSystems, v. 13, p. 243-251",
    note = "talkorigins\_source = {true}; raw\_reference = {Ishima, Y., Pryzbylski, A., and Fox, S. W., 1981, Electrical membrane phenomena in spherules from protenoid and lecithin: BioSystems, v. 13, p. 243-251.}"
}

@article{doi101023a1018992924025,
    author = "Santiago, Noemi and Milstein, Sam and Rivera, Theresa and García, Elisa and Zaidi, Tabassum and Hong, H K and Bucher, Doris J.",
    title = "Oral Immunization of Rats with Proteinoid Microspheres Encapsulating Influenza Virus Antigens",
    year = "1993",
    journal = "Pharmaceutical Research",
    url = "https://doi.org/10.1023/a:1018992924025",
    doi = "10.1023/a:1018992924025",
    openalex = "W114505501",
    references = "doi101007978147572046418, doi10100797836427452946, doi101007bf00915547, doi101016016158909190076v, doi101038280147a0, doi101056nejm198307073090103, doi101128iai363110211081982, doi101128jcm23166721986, doi101146annurevmi37100183002525, openalexw2409929920"
}

@article{doi101016s0142961297001889,
    author = "Kumar, Anurag and Rao, K. Panduranga",
    title = "Preparation and characterization of pH-sensitive proteinoid microspheres for the oral delivery of methotrexate",
    year = "1998",
    journal = "Biomaterials",
    url = "https://doi.org/10.1016/s0142-9612(97)00188-9",
    doi = "10.1016/s0142-9612(97)00188-9",
    openalex = "W2041007310"
}

@article{doi101007bfb0018078,
    author = "Nakashima, Tadayoshi",
    title = "Metabolism of proteinoid microspheres",
    year = "2005",
    journal = "Topics in Current Chemistry",
    url = "https://doi.org/10.1007/bfb0018078",
    doi = "10.1007/bfb0018078",
    openalex = "W1533658605",
    references = "doi101007bf00405480, doi101007bf00623555, doi101007bf01732668, doi1010160303264780900131, doi101016b9781483228617500284, doi101016s0047248478800529, doi101021ja00438a050, doi101021ja01499a069, doi1010382031362a0, doi101038244418a0, openalexw2983085323"
}

@article{doi101002ijch201800021,
    author = "Kolitz‐Domb, Michal and Margel, Shlomo",
    title = "Recent Advances of Novel Proteinoids and Proteinoid Nanoparticles and Their Applications in Biomedicine and Industrial Uses",
    year = "2018",
    journal = "Israel Journal of Chemistry",
    abstract = "Abstract Proteinoids, thermal polymers composed of amino acids, discovered and studied by Fox, spontaneously self‐assemble in spherical structures, microspheres, which Fox presented as the protocells of life. Fox's findings opened up a scope of applicable easy‐to‐make protein‐like particles. In recent years, interest in proteinoids has increased among nanobiomedicine research workers. These structures are suitable for biomedical applications, due to their protein‐like nature, biocompatibility, non‐toxicity and safety. Several new proteinoids made of a specific selection of amino acids were introduced for biomedical and agricultural industries. Several proteinoids include specific additives polymerized within their backbone, providing special chracteristics for a specific application. These proteinoids, their corresponding nanoparticles and their diverse applications are presented here, primarily focusing on proteinoids for cancer diagnostics and therapy, cosmetic and anti‐fog proteinoids.",
    url = "https://doi.org/10.1002/ijch.201800021",
    doi = "10.1002/ijch.201800021",
    openalex = "W2898478618",
    references = "doi101007bfb0018078, doi101016jaddr200410009, doi101016jaddr200903009, doi101016jbiomaterials201209027, doi101016jcis200605026, doi101016jjconrel201203020, doi101021nn1005232, doi10118621623619110, doi101208s1224800890712, doi1021650000308820034205000002, fox1958thermal, fox1960thermal"
}

@article{doi101021acsomega9b00336,
    author = "Sason, Elisheva and Kolitz‐Domb, Michal and Chill, Jordan H. and Margel, Shlomo",
    title = "Engineering of Durable Antifog Thin Coatings on Plastic Films by UV-Curing of Proteinoid Prepolymers with PEG-Diacrylate Monomers",
    year = "2019",
    journal = "ACS Omega",
    abstract = "Fog formation on transparent surfaces constitutes a major challenge in several optical applications, such as plastic packaging, lenses, mirrors, and windshields. To overcome this problem, we prepared and characterized durable antifog thin coatings on plastic films such as polyethylene terephthalate (PET). Proteinoids are biocompatible random polymers made of α-amino acids by thermal step-growth polymerization. Proteinoid prepolymers were prepared by adding activated double bonds to proteinoids via the Michael addition reaction. A series of thin antifog cross-linked coatings were prepared by spreading on PET films with a Mayer rod various mixtures of the proteinoid prepolymers, polyethylene glycol diacrylate, and a photoinitiator, followed by UV-curing of the dried coatings. The antifog properties of the coatings were determined by the contact angle, roughness, haze, and gloss measurements, as well as hot and cold fog tests, to examine the optical properties of the films under fog formation conditions. Mechanical properties such as adhesion, robustness, and abrasion resistance of the antifog coatings were examined by tape, knife-scratch, and sandpaper abrasion tests. The effect of coating composition, wettability, and roughness on the antifog properties of the coated PET films was elucidated. The formula was optimized, and the corresponding UV-cured antifog cross-linked thin coating exhibited transparency with good adhesion and excellent durable antifog performance.",
    url = "https://doi.org/10.1021/acsomega.9b00336",
    doi = "10.1021/acsomega.9b00336",
    openalex = "W2946868506",
    references = "doi101007978940102239219, doi101007bf00927027"
}

@article{doi101186s1295102000709z,
    author = "Lugasi, Liroy and Grinberg, Igor and Rudnick‐Glick, Safra and Okun, Eitan and Einat, Haim and Margel, Shlomo",
    title = "Designed proteinoid polymers and nanoparticles encapsulating risperidone for enhanced antipsychotic activity",
    year = "2020",
    journal = "Journal of Nanobiotechnology",
    abstract = "Proteinoid NPs enhance RSP delivery and may potentially increase drug efficiency by reducing dosage and side effects.",
    url = "https://doi.org/10.1186/s12951-020-00709-z",
    doi = "10.1186/s12951-020-00709-z",
    openalex = "W3093880023",
    references = "doi101002ijch201800021, doi101002qua560220719, doi101007978940102239219"
}

@article{doi101016jbiosystems2023104892,
    author = "Mougkogiannis, Panagiotis and Phillips, Neil and Adamatzky, Andrew",
    title = "Transfer functions of proteinoid microspheres",
    year = "2023",
    journal = "Biosystems",
    abstract = "Proteinoids, or thermal proteins, are inorganic entities formed by heating amino acids to their melting point and commencing polymerisation to form polymeric chains. Typically, their diameters range from 1μm to 10μm. Some amino acids incorporated into proteinoid chains are more hydrophobic than others, leading proteinoids to cluster together when they are present in aqueous solutions at specific concentrations, allowing them to grow into microspheres. The peculiar structure of proteinoids composed of linked amino acids endows them with unique properties, including action-potential like spiking of electrical potential. These unique properties make ensembles of proteinoid microspheres a promising substrate for designing future artificial brains and unconventional computing devices. To evaluate a potential of proteinoid microspheres for unconventional electronic devices we measure and analyse the data-transfer capacities of proteinoid microspheres. In experimental laboratory conditions we demonstrate that the transfer function of proteinoids microspheres is a nontrivial phenomenon, which might be due to the wide range of proteinoid shapes, sizes, and structures.",
    url = "https://doi.org/10.1016/j.biosystems.2023.104892",
    doi = "10.1016/j.biosystems.2023.104892",
    openalex = "W4366133631",
    references = "doi101007bf00927027, doi1010160303264771900037, doi1010160303264781900046, doi101016jbiosystems2021104480, doi101016jjpowsour200511035, doi101021bi00489a038, doi101038nmat4148, doi101038nnano200818, doi101038s4157801900890, doi101039df9470100011, doi101039f29868200075, doi10110916725254"
}

@article{doi101016jbiosystems2023105015,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Light induced spiking of proteinoids",
    year = "2023",
    journal = "Biosystems",
    abstract = "Proteinoids, or thermal proteins, are produced by heating amino acids to their melting point and initiating polymerisation to produce polymeric chains. In aqueous solutions proteinoids swell into hollow microspheres. These microspheres produce endogenous burst of electrical potential spikes and change patterns of their electrical activity in response to illumination. We report results on a detailed investigation on the effects of white cold light on the spiking of proteinoids. We study how different types and intensities of light determine proteinoids' spiking amplitude, period, and pattern. The results of this study will be utilised to evaluate proteinoids for their potential as optical sensors and their application in unconventional computing.",
    url = "https://doi.org/10.1016/j.biosystems.2023.105015",
    doi = "10.1016/j.biosystems.2023.105015",
    openalex = "W4386295585",
    references = "doi101002ijch201800021, doi101016jbiosystems2023104892"
}

@article{doi101016jmatdes2023112460,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Light-induced spiking in proteinoids yields Boolean gates",
    year = "2023",
    journal = "Materials \& Design",
    abstract = "This study analyzes light modulation of spiking in proteinoids, thermally condensed proteins exhibiting spike dynamics. We elucidate how light induces changes in proteinoids, modulating spike frequency. Results show proteinoids' spiking can be adjusted by light intensity and wavelength. Structural investigations demonstrate light triggers conformational changes influencing spiking kinetics. Spiking proteinoids can perform Boolean logic, generating programmable expressions in response to light input modifications. This reveals potential unconventional computing applications. Our comprehensive analyses establish a fundamental understanding of light's impact on proteinoids' structure and protrusion dynamics, facilitating optically programmed bio-logic gates. Outcomes will catalyze future research into light-modified proteinoids for information processing and unconventional computation. In summary, this study provides key insights into light modulation of proteinoids' spiking behavior, enabling novel optically controlled bio-logic gate operations and motivating continued efforts to integrate photo-responsive proteinoids in bioinspired computational systems.",
    url = "https://doi.org/10.1016/j.matdes.2023.112460",
    doi = "10.1016/j.matdes.2023.112460",
    openalex = "W4388672841",
    references = "doi1010160303264771900037"
}

@article{doi101021acsomega3c05670,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Proteinoid Microspheres as Protoneural Networks",
    year = "2023",
    journal = "ACS Omega",
    abstract = "Proteinoids, also known as thermal proteins, possess a fascinating ability to generate microspheres that exhibit electrical spikes resembling the action potentials of neurons. These spiking microspheres, referred to as protoneurons, hold the potential to assemble into proto-nanobrains. In our study, we investigate the feasibility of utilizing a promising electrochemical technique called differential pulse voltammetry (DPV) to interface with proteinoid nanobrains. We evaluate DPV's suitability by examining critical parameters such as selectivity, sensitivity, and linearity of the electrochemical responses. The research systematically explores the influence of various operational factors, including pulse width, pulse amplitude, scan rate, and scan time. Encouragingly, our findings indicate that DPV exhibits significant potential as an efficient electrochemical interface for proteinoid nanobrains. This technology opens up new avenues for developing artificial neural networks with broad applications across diverse fields of research.",
    url = "https://doi.org/10.1021/acsomega.3c05670",
    doi = "10.1021/acsomega.3c05670",
    openalex = "W4386692072",
    references = "crossref1998exobiology, doi101002qua560220719, doi101007978364277211512, doi1010160026265x73901124, doi101016jbiosystems2023104892, doi101021ja01544a027, doi101179isr1988134348"
}

@article{doi101098rsos230936,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Learning in ensembles of proteinoid microspheres",
    year = "2023",
    journal = "Royal Society Open Science",
    abstract = "Proteinoids are thermal proteins which form microspheres in water in the presence of salt. Ensembles of proteinoid microspheres exhibit passive nonlinear electrical properties and active neuron-like spiking of electrical potential. We propose that various neuromorphic computing architectures can be prototyped from the proteinoid microspheres. A key feature of a neuromorphic system is a learning. Through the use of optical and resistance measurements, we study mechanisms of learning in ensembles of proteinoid microspheres. We analyse 16 types of proteinoids study and their intrinsic morphology and electrical properties. We demonstrate that proteinoids can learn, memorize and habituate, making them a promising candidate for novel computing.",
    url = "https://doi.org/10.1098/rsos.230936",
    doi = "10.1098/rsos.230936",
    openalex = "W4387538421",
    references = "doi101007978364277211512, doi101016jbiosystems2023104892"
}

@article{doi101371journalpone0289433,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Logical gates in ensembles of proteinoid microspheres",
    year = "2023",
    journal = "PLoS ONE",
    abstract = "Proteinoids are thermal proteins which swell into microspheres in aqueous solution. Ensembles of proteinoids produce electrical spiking activity similar to that of neurons. We introduce a novel method for implementing logical gates in the ensembles of proteinoid microspheres using chronoamperometry. Chronoamperometry is a technique that involves applying a voltage pulse to proteinoid microspheres and measuring their current response. We have observed that proteinoids exhibit distinct current patterns that align with various logical outputs. We identify four types of logical gates: AND, OR, XOR, and NAND. These gates are determined by the current response of proteinoid microspheres. Additionally, we demonstrate that proteinoid microspheres have the ability to modify their current response over time, which is influenced by their previous exposure to voltage. This indicates that they possess a capacity for learning and are capable of adapting to their environment. Our research showcases the ability of proteinoid microspheres to perform logical operations and computations through their inherent electrical properties.",
    url = "https://doi.org/10.1371/journal.pone.0289433",
    doi = "10.1371/journal.pone.0289433",
    openalex = "W4386839866",
    references = "doi101016jbiosystems2023104892"
}

@article{doi101007s12668024016785,
    author = "Mougkogiannis, Panagiotis and Nikolaidou, Anna and Adamatzky, Andrew",
    title = "On Emergence of Spontaneous Oscillations in Kombucha and Proteinoids",
    year = "2024",
    journal = "BioNanoScience",
    abstract = "An important part of studying living systems is figuring out the complicated steps that lead to order from chaos. Spontaneous oscillations are a key part of self-organisation in many biological and chemical networks, including kombucha and proteinoids. This study examines the spontaneous oscillations in kombucha and proteinoids, specifically exploring their potential connection to the origin of life. As a community of bacteria and yeast work together, kombucha shows remarkable spontaneous oscillations in its biochemical parts. This system can keep a dynamic balance and organise itself thanks to metabolic processes and complex chemical reactions. Similarly, proteinoids, which may have been primitive forms of proteins, undergo spontaneous fluctuations in their structure and function periodically. Because these oscillations happen on their own, they may play a very important part in the development of early life forms. This paper highlights the fundamental principles governing the transition from chaos to order in living systems by examining the key factors that influence the frequency and characteristics of spontaneous oscillations in kombucha and proteinoids. Looking into these rhythms not only helps us understand where life came from but also shows us ways to make self-organising networks in synthetic biology and biotechnology. There is significant discussion over the emergence of biological order from chemical disorder. This article contributes to the ongoing discussion by examining at the theoretical basis, experimental proof, and implications of spontaneous oscillations. The results make it clear that random oscillations are an important part of the change from nonliving to living matter. They also give us important information about what life is all about.",
    url = "https://doi.org/10.1007/s12668-024-01678-5",
    doi = "10.1007/s12668-024-01678-5",
    openalex = "W4405028317",
    references = "doi101007978364277211512, doi101007bf01797193, doi1010160303264771900037, doi1010160303264780900131, doi1010160303264781900046, doi101016jbiosystems2023104892, doi10103835002125, doi101038nrn2201, doi101073pnas982676, doi101093acprofoso97801953010690010001, doi101103revmodphys65851, doi101103revmodphys70223, doi101126science1173046528, doi101146annurevneuro071013014030, doi101351pac197334030641, fox1995thermal, openalexw2991415348"
}

@article{doi101016jmtbio2024100989,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Recognition of sounds by ensembles of proteinoids",
    year = "2024",
    journal = "Materials Today Bio",
    abstract = "Proteinoids are artificial polymers that imitate certain characteristics of natural proteins, including self-organization, catalytic activity, and responsiveness to external stimuli. This paper examines the acoustic response properties of proteinoids microspheres when exposed to auditory stimuli. We convert sounds of English alphabet into waveforms of electrical potential, feed the waveforms into proteinoid solutions and record electrical responses of the proteinoids. We also undertake a detailed comparison of proteinoids' electrical responses (frequencies, periods, and amplitudes) with original input signals. We found that responses of proteinoids are less regular, lower dominant frequency, wider distribution of proteinoids and less skewed distribution of amplitudes compared with input signals. We found that resonant acoustic excitation of proteinoids generates unique electrical impulse patterns dependent on sound frequency and amplitude. The finding will be used in further designs of organic electronic devices, based on ensembles of proteinoids, for sound processing and speech recognition. Our findings provide the first quantitative investigation into the potential of thermal proteinoid microspheres for bio-inspired sound processing and recognition applications. Using controlled speaker excitation on proteinoid samples, we create reliable markers of productive acoustic response capacities, paving the way for future advancement.",
    url = "https://doi.org/10.1016/j.mtbio.2024.100989",
    doi = "10.1016/j.mtbio.2024.100989",
    openalex = "W4391788360",
    references = "doi1010160303264780900131, doi101016jbiosystems2023104892"
}

@article{doi101016jrechem2024101950,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Influence of proteinoids on calcium carbonate polymorphs precipitation in supersaturated solutions",
    year = "2024",
    journal = "Results in Chemistry",
    abstract = "• Proteinoid microspheres show neuron-like electrical activity and can form information- processing networks, functioning as proto-brains. • Calcium carbonate crystals enhance microspheres' electrical properties and serve as scaffolds to improve their connectivity. • The research advances bio-computing and origin-of-life studies by examining how proteinoid-based structures function. Proteinoids, or thermal proteins, are amino acid polymers formed at high temperatures by non-biological processes. Pro- teinoids form microspheres in liquids. The microspheres exhibit electrical activity similar to that of neurons. The electrically spiking microspheres are seen as proto-neurons capable of forming networks and carrying out information transmission and processing. Previously, we demonstrated that ensembles of proteinoid microspheres can respond to optical and electrical stimulation, implement logical gates, recognise arbitrary wave forms, and undergo learning. Thus, the ensembles of proteinoid microspheres can be seen as proto-brains. In present paper we decided to uncover morphologies of these proto-brains. We utilise a supersaturated solution of calcium carbonate to facilitate the crystallisation of proteinoids and subsequently generate proteinoid brain structures. Our hypothesis suggests that calcium carbonate crystals have the potential to serve as scaffolds and connectors for proteinoid microspheres, thereby improving their electrical properties and facilitating communication. In this section, we outline the experimental methods and techniques used in our study. We share our findings and results regarding the morphology, composition, stability, and functionality of proteinoid brain structures. We discuss the implications and applications of our work in the fields of bio-inspired computing, artificial neural networks, and origin of life research.",
    url = "https://doi.org/10.1016/j.rechem.2024.101950",
    doi = "10.1016/j.rechem.2024.101950",
    openalex = "W4405527870",
    references = "doi1010160303264771900037"
}

@article{doi101016jijbiomac2025146385,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Scale-dependent analysis of structure and electrical activity in kombucha mats and proteinoid–actin assemblies",
    year = "2025",
    journal = "International Journal of Biological Macromolecules",
    abstract = "This study examines, in detail, the scale-dependent properties and activity patterns in two systems: kombucha cultures and proteinoid-actin networks. These systems have complex features. Our analysis shows that their self-similarity may not be a true fractal at all scales. The kombucha pellicle is not fractal in shape. However, it shows electrical activity with a fractal-like pattern. In contrast, proteinoid-actin assemblies have hierarchical clustering. But they lack consistent self-similarity at different scales. Both systems show nonlinear thermosensory responses. Temperature changes induce complex behavioural and structural changes. The electrical activity in kombucha cultures shows chaotic dynamics. It is sensitive to initial conditions and has self-organized criticality. This study on kombucha cultures and proteinoid-actin networks offers new insights. It highlights the key difference between fractal-like patterns and true fractal geometry in biological systems. The research shows that complex organization and varying electrical activity can occur without self-similarity at every scale. It distinguishes true fractal organization from complex hierarchies in biological and prebiotic systems. These findings enhance our understanding of complex biology. They may contribute to our understanding of biomimetic materials science and synthetic biology. This is especially true for the role of electrical activity patterns in self-organizing systems.",
    url = "https://doi.org/10.1016/j.ijbiomac.2025.146385",
    doi = "10.1016/j.ijbiomac.2025.146385",
    openalex = "W4413113080",
    references = "doi101002advs202506155, doi101007s12668024016785, doi101016b9780123361561500616, doi101016jcarpta2024100627, doi101016s0006349561869026, doi101021acsomega5c01141, doi101021es0605016, doi101038nmeth2089, doi10106314823332, doi101109jiot20162579198, doi101109jrproc1962288235, doi101109tsmc19794310076, doi101126science1070821, doi107551mitpress25260010001"
}

@article{doi101021acsabm5c00964,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Spiking Neurons Derived from Proteinoid and Bacteriorhodopsin",
    year = "2025",
    journal = "ACS Applied Bio Materials",
    abstract = "We investigate proteinoid-bacteriorhodopsin complexes as biomolecular spiking neurons for neuromorphic computing applications. Our system shows strong photoresponsive behavior through the integration of bacteriorhodopsin with self-assembled proteinoid structures. Measurements show that proteinoid-bacteriorhodopsin complexes have greater electrical activity (10.77 ± 2.21 mV) than proteinoids alone (4.34 ± 4.47 mV). The complexes have wavelength-dependent responses to 5 Hz optical stimulation. Green light (λ ≈ 520 nm) produced the strongest amplitude (7.31 ± 1.49 mV). Temporal analysis shows a consistent periodicity (τ ≈ 645 s) across wavelengths. This indicates stable oscillatory mechanisms. Random walk computations show distinct spatiotemporal patterns, suggesting potential applications in light-controlled molecular computing. These findings demonstrate that proteinoid-bacteriorhodopsin complexes are promising candidates for bioinspired computing and offer possibilities for developing biomolecular information systems.",
    url = "https://doi.org/10.1021/acsabm.5c00964",
    doi = "10.1021/acsabm.5c00964",
    openalex = "W4413292799",
    references = "doi101002advs202506155, doi101006jmbi19993027, doi101007s0042500807727, doi101016jnantod200810014, doi101016s0006349575858759, doi101021acsomega5c01141, doi101021cr4003769, doi101038newbio233149a0, doi101038nmethf324, doi101126science1925597, doi101146annurevbiochem671653, doi101146annurevneuro061010113817, doi101371journalpone0324761"
}

@article{doi101021acschemneuro4c00801,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Serotonergic Mechanisms in Proteinoid-Based Protocells",
    year = "2025",
    journal = "ACS Chemical Neuroscience",
    abstract = "This study examines the effects of incorporating serotonin (5-HT) into proteinoid microspheres. It looks at the microspheres' structure and electrochemical properties. Proteinoid-serotonin assemblies have better symmetry and membrane organization than pristine proteinoids. Cyclic voltammetry shows a big boost in electron transfer. This is proven by a smaller peak separation and higher electrochemical efficiency. SEM imaging shows a distinct core-shell structure and uniform density. This suggests ordered molecular assembly. These findings show that serotonin changes proteinoid self-assembly. It creates structured systems with better electron transfer pathways. The serotonin-modified proto-neurons show new properties. They give insights into early cellular organization and signaling. This helps us understand prebiotic information processing systems.",
    url = "https://doi.org/10.1021/acschemneuro.4c00801",
    doi = "10.1021/acschemneuro.4c00801",
    openalex = "W4406696823",
    references = "doi101007bf02301336, doi101016jbiosystems2023104892, doi103390biomimetics9070380"
}

@article{doi101021acsomega5c01141,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Self-Organizing Proteinoid-Actin Networks: Structure and Voltage Dynamics.",
    year = "2025",
    journal = "ACS omega",
    abstract = "Proteinoids are thermal proteins produced by heating amino acids to their melting point and initiation of polymerization to produce polymeric chains. Proteinoids swell in aqueous solution forming hollow microspheres, usually filled with aqueous solution. The microspheres produce spikes of electrical potential similar to the action potentials of living neurons. The cytoskeletal protein actin is known in its filamentous form as F-actin. Filaments are organized in a double helix structure consisting of polymerized globular actin monomers. Actin is a protein that is abundantly expressed in all eukaryotic cells and plays a crucial role in cellular functions by forming an intracellular scaffold, actuators, and pathways for information transfer and processing. We produce and study proteinoid-actin networks as physical models of primitive neurons. We look at their structure and electrical dynamics. We use scanning electron microscopy and multichannel electrical recordings to study microsphere assemblies. They have distinct surface features, including ion channel-like pores. The proteinoid-actin mixture exhibits enhanced electrical properties compared to its individual components. Its conductivity (σ = 4.68 × 10-4 S/cm) is higher than those of both pure actin (σ = 1.23 × 10-4 S/cm) and pure proteinoid (σ = 2.45 × 10-4 S/cm). The increased conductivity and new oscillatory patterns suggest a synergy. They indicate a synergy between the proteinoid and actin components in the mixture. Multichannel analysis reveals type I regular spiking in proteinoid networks (ΔV ≈ 50 mV, τ = 52.4 s), type II excitability in actin (V max ≈ 40 mV), and bistable dynamics in the mixture. These findings suggest that proteinoid-actin complexes can form primitive bioelectrical systems. This might lead to the better understanding of the evolution of the primordial neural system.",
    url = "https://pmc.ncbi.nlm.nih.gov/articles/PMC12079275/",
    doi = "10.1021/acsomega.5c01141",
    openalex = "W4410096193",
    pmcid = "PMC12079275",
    pmid = "40385176",
    references = "doi101016s030744129800065x, doi101038nature08908, doi101038sjnpp1301559, doi101073pnas0408930102, doi10112114776777, doi101126science1174621, doi101126science1175862, doi101142s0129065709002002, doi101194jlrr200021jlr200, doi1012019781315735368"
}

@article{doi101371journalpone0324761,
    author = "Mougkogiannis, Panagiotis and Ghadafi, Essam and Adamatzky, Andrew",
    title = "Bio-inspired cryptography based on proteinoid assemblies",
    year = "2025",
    journal = "PLoS ONE",
    abstract = "We present an innovative cryptographic technique inspired by the self-assembly processes of proteinoids-thermally stable proteins that form spontaneously under prebiotic conditions. By emulating the deterministic yet complex interactions within proteinoid assemblies, the proposed method generates secure encryption keys and algorithms. We measure the unique electrical properties of proteinoid microspheres. Their capacitance values range from -656.6 to 434.9 nF. Then, we convert these measurements into encryption keys using the formula [Formula: see text]. The approach harnesses the inherent unpredictability of proteinoid behavior to create a robust and adaptable encryption framework resilient to cryptanalytic attacks. The encryption process uses modular multiplication: [Formula: see text] [Formula: see text] [Formula: see text]. This changes plaintext into ciphertext. The security relies on electrical signatures that depend on the composition. Experimental results show that this bio-inspired system aligns with contemporary encryption standards, offering significant benefits in key generation and distribution. Our implementation has a linear computational complexity of O(n). It offers security levels ranging from 8 to 128 bits, based on composition. Additionally, it is energy efficient, performing about 200 operations per joule. Statistical analysis further affirms the high randomness of the generated keys, highlighting the potential of biological processes in advancing cryptographic security.",
    url = "https://doi.org/10.1371/journal.pone.0324761",
    doi = "10.1371/journal.pone.0324761",
    openalex = "W4410809340",
    references = "doi101016jbiosystems2023104892, doi101016jpatcog201401016, doi101016jswevo201904008, doi101021nl071804g, doi101038382525a0, doi101038nature23461, doi1010800161110291890876, doi101126science1093669, doi101126science183412046, doi1022331q2018080679, doi105120115077224, fox1995thermal"
}

@article{doi103390biomimetics10060360,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Polymorphism in Glu-Phe-Asp Proteinoids",
    year = "2025",
    journal = "Biomimetics",
    abstract = "Glu-Phe-Asp (GFD) proteinoids represent a class of synthetic polypeptides capable of self-assembling into microspheres, fibres, or combinations thereof, with morphology dramatically influencing their electrical properties. Extended recordings and detailed waveforms demonstrate that microspheres generate rapid, nerve-like spikes, while fibres exhibit consistent and gradual variations in voltage. Mixed networks integrate multiple components to achieve a balanced output. Electrochemical measurements show clear differences. Microspheres have a low capacitance of 1.926±5.735μF. They show high impedance at 6646.282±178.664 Ohm. Their resistance is low, measuring 15,830.739 ± 652.514 mΩ. This structure allows for quick ionic transport, leading to spiking behaviour. Fibres show high capacitance (9.912±0.171μF) and low impedance (209.400±0.286 Ohm). They also have high resistance (163,067.613 ± 9253.064 mΩ). This combination helps with charge storage and slow potential changes. The 50:50 mixture shows middle values for all parameters. This confirms that hybrid electrical properties have emerged. The differences come from basic structural changes. Microspheres trap ions in small, round spaces. This allows for quick release. In contrast, fibers spread ions along their length. This leads to slower wave propagation. In mixed systems, diverse voltage zones emerge, suggesting cooperative dynamics between morphologies. This electrical polymorphism in simple proteinoid systems may explain complexity in biological systems. This study shows that structural polymorphism in GFD proteinoids affects their electrical properties. This finding is significant for biomimetic computing and sheds light on prebiotic information-processing systems.",
    url = "https://doi.org/10.3390/biomimetics10060360",
    doi = "10.3390/biomimetics10060360",
    openalex = "W4410999463",
    references = "doi101002ijch201800021, doi101016jbiosystems2023104892, doi103390biomimetics9070380"
}

@article{doi101021acslangmuir6c00952,
    author = "Mougkogiannis, Panagiotis and Adamatzky, Andrew",
    title = "Proteinoid Computing on Olivine Substrates",
    year = "2026",
    journal = "Langmuir",
    abstract = "We investigate proteinoid systems formed on olivine mineral substrates, focusing on self-organization, electrochemical properties, and information-processing capacity. Olivine's ubiquity in meteorites, planetary surfaces, and protoplanetary disks makes it a geochemically relevant template for prebiotic chemistry across cosmic environments. Glu:Phe:Asp proteinoids synthesized in olivine-rich acidic solutions─mimicking early Earth hydrothermal conditions─were characterized using scanning electron microscopy (SEM), electrochemical impedance spectroscopy (EIS), cyclic voltammetry (CV), and differential pulse voltammetry (DPV). The proteinoids self-assembled into spherical microspheres (2-15 μm in diameter), dendritic networks, and complex mineral-templated architectures. Budding-like reproduction and neuron-like branching morphologies emerged spontaneously. Electrochemical analysis revealed stable impedance profiles that, when thresholded, enabled Boolean logic operations (AND, OR, XOR, and NOT). Galvanostatic measurements showed spontaneous electrical oscillations with burst dynamics, heavy-tailed distributions, and non-Poissonian statistics, which are signatures of complex adaptive systems. Olivine substrates stabilized the electrical behavior while preserving computational functionality. These findings suggest that proteinoid-olivine hybrids can perform unconventional computing tasks while simultaneously exhibiting biomimetic self-assembly and primitive reproductive behaviors. This work illuminates mineral-organic interactions relevant to both terrestrial and extraterrestrial prebiotic chemistry and provides a foundation for bioinspired computing systems that merge organic self-organization with mineral-based information processing.",
    url = "https://doi.org/10.1021/acs.langmuir.6c00952",
    doi = "10.1021/acs.langmuir.6c00952",
    openalex = "W7141461542",
    references = "doi101002advs202506155, doi10100797814613251544, doi101007s12668024016785, doi101016jcarpta2024100627, doi101021acsabm5c00964, doi101371journalpone0324761"
}