From proteinoid microsphere to contemporary cell: Formation of internucleotide and peptide bonds by proteinoid particles

Fox, Sidney W.; Jungck, John R.; Nakashima, Tadayoshi

doi:10.1007/bf00927027

Cited by 70 publications

(29 citation statements)

References 17 publications

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“…Proteinoids are polymers made of natural amino acids by thermal step-growth polymerization, studied by Fox and coworkers six decades ago. [1] Fox studied the origin of life, exploring the synthesis of amino acid polymers from inorganic molecules and thermal energy, creating what he thought of as the world's first protocell, made of his proteinoids and water. Fox believed in a process of abiogenesis, where life spontaneously organized itself from a "primordial soup", pools of various simple organic molecules that existed before life on Earth.…”

Section: Introductionmentioning

confidence: 99%

Recent Advances of Novel Proteinoids and Proteinoid Nanoparticles and Their Applications in Biomedicine and Industrial Uses

Kolitz‐Domb

Margel

2018

Israel Journal of Chemistry

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Proteinoids, thermal polymers composed of amino acids, discovered and studied by Fox, spontaneously selfassemble 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.

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Section: Introductionmentioning

confidence: 99%

Recent Advances of Novel Proteinoids and Proteinoid Nanoparticles and Their Applications in Biomedicine and Industrial Uses

Kolitz‐Domb

Margel

2018

Israel Journal of Chemistry

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“…[italics added] In the model-building of primordial systems, the biochemical premise of enzymes (protein)-first was tested [20]. The nonrandom products, proteinoids, result from self-ordering of amino acids [2 11; basic ones catalyze the synthesis of both peptide and intemucleotide bonds [22,23].…”

Section: Discussionmentioning

confidence: 99%

Reproducibility of amino acid compositions in repeated copolymerizations of amino acids

Fox

Windsor

1984

Int. J. Quantum Chem.

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Amino acid analysis has been performed on the products of four simultaneous separate thermal copolymerizations of a set of 18 amino acids. Four analyses have been performed also on aliquots of one of the products. Standard deviations have been calculated for the analyses of the products of the four separate copolymerizations, and for the four aliquots of one copolymerization. All calculations indicate a high reproducibility in the copolymerization reactions.

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“…In addition the presence of a moderately hydrophobic microenvironment may have enhanced the interactions of the polar amino acyl adenylates with polynucleotide bases, since polar interactions would be stronger in regions of low dielectric constant. Fox et al (1974) also reported a slight yield of oligomers from phenylalanine reacting with ATP, Poly A, and lysine-rich proteinoids, whereas other combinations gave no peptides. The simultaneous formation of peptides and oligonucleotides in a hypohydrous environment produced low selectivities among the various (oligo) nucleotide bases in their effects on peptide yields.…”

Section: Offprint Requests To: Dh Whitementioning

confidence: 92%

Enhancement of peptide bond formation by polyribonucleotides on clay surfaces in fluctuating environments

White

Erickson

1981

J Mol Evol

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Summary. The condensation of glycine to form oligoglycine during temperature and moisture fluctuations on clay surfaces was enhanced up to fourfold by polyribonucleotides. Polydeoxyribonucleotides gave no enhancement. Yields were greatly reduced in the absence of clay. A small preference was observed among the polyribonucleotide bases with enhancements in the order of Poly G > Poly A = Poly U > Poly C at high density of polynucleotide on the clay surface and Poly G > Poly U > Poly C > Poly A at low density. This and other experiments seem to indicate a codonic bias in the interaction of polynucleotides with amino acids reacting to form peptide bonds. A mechanism is proposed which involves (1) activation of glycine on the clay surface, (2) formation of esters between glycine and the 2'-OH groups of the polyribonucleotide, and (3) formation of peptide bonds between adjacent amino acyl esters. If this mechanism is correct, it may provide the basis for a simple, direct-template translation process.

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From proteinoid microsphere to contemporary cell: Formation of internucleotide and peptide bonds by proteinoid particles

Cited by 70 publications

References 17 publications

Recent Advances of Novel Proteinoids and Proteinoid Nanoparticles and Their Applications in Biomedicine and Industrial Uses

Recent Advances of Novel Proteinoids and Proteinoid Nanoparticles and Their Applications in Biomedicine and Industrial Uses

Reproducibility of amino acid compositions in repeated copolymerizations of amino acids

Enhancement of peptide bond formation by polyribonucleotides on clay surfaces in fluctuating environments

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