Compartmentalization in proteinoid microspheres

Brooke, Steven; Fox, Sidney W.

doi:10.1016/0303-2647(77)90028-4

Cited by 29 publications

(18 citation statements)

References 13 publications

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“…The microspheres made from both kinds of proteinoid have been shown by staining to contain both kinds of proteinoid, but the two are not uniformly distributed [48]. The "acidic-basic'' microspheres are also the kind that proved to be indistinguishable from artificial fossils of algae [49, cf.…”

Section: Lysine-rich Proteinoid Can Be Coaggregated Into Proteinoid Mmentioning

confidence: 99%

“…Compartmentalization, as Matsuno states [ 591, arises easily in proteinoid microspheres [48]. It is conditioned by cations such as calcium, and by a combination of acidic and lysine-rich proteinoids.…”

Section: Compartmentalizationmentioning

confidence: 99%

“…The hypercycle is a principle of natural self-organization, which phenomenon is also displayed by proteinoid systems, as titles of reviews indicate [ 12, 131. Both hypercycles and "metabolic microspheres" [29] relate to some of the same phenomena, e.g., compartmentalization [48]. Eigen and Schuster regard Darwin's principle of natural selection as a second principle of material self-organization [24].…”

Section: Epiloguementioning

confidence: 99%

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Origins of the protein synthesis cycle

Fox

1981

Int. J. Quantum Chem.

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Largely derived from experiments in molecular evolution, a theory of the origins of protein synthesis cycles has been constructed. The sequence begins with ordered thermal proteins resulting from the self-sequencing of mixed amino acids. Ordered thermal proteins then aggregate to cell-like structures. When they contained proteinoids sufficiently rich in lysine, the structures were able to synthesize offspring peptides. Since lysine-rich proteinoid (LRP) also catalyzes the polymerization of nucleoside triphosphate to polynucleotides, the same microspheres containing LRP could have synthesized both original cellular proteins and cellular nucleic acids. The LRP within protocells would have provided proximity advantageous for the origin and evolution of the genetic code.

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Section: Lysine-rich Proteinoid Can Be Coaggregated Into Proteinoid Mmentioning

confidence: 99%

Section: Compartmentalizationmentioning

confidence: 99%

Section: Epiloguementioning

confidence: 99%

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Origins of the protein synthesis cycle

Fox

1981

Int. J. Quantum Chem.

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“…Some of the evolutionary interest in proteinoids has continued with the later work of Matsuno21 and Fox 22. A proteinoid can be swelled in a buffer (or water) at moderate temperatures (usually around 50°C) forming a microsphere structure (e.g., Ref 23…”

Section: Introductionmentioning

confidence: 99%

New polymer syntheses part: 54 novel conducting polymers and copolymers based on 4‐Teriary butyl‐cyclohexanone moiety in the main chain

Aly

2011

J of Applied Polymer Sci

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A new interesting class of conducting polymer and copolymers based on 4-teriary butyl-cyclohexanone in the main chain has been synthesized by solution polycodensation of terephthalaldehyde with 4-teriary butylcyclohexanone and/or cycloalkanone derivatives. The model compound I was synthesized from the 4-teriary butyl-cyclohexanone with benzaldehyde, and its structure was confirmed by elemental and spectral analyses. The resulting polymer and copolymers were characterized by elemental and spectral analyses including Fourier transform infrared spectrometer (FT-IR) and nuclear magnetic resonance ( 1 H-NMR), beside solubility and viscometry measurements. The thermal properties of those polymer and copolymers were evaluated by thermogravimetric analysis (TGA) and differential scanning calorimeter (DSC) measurements and correlated to their structural units. X-ray analysis showed that it has some degree of crystallinity in the region 2y ¼ 5-60. The UV-visible spectra of some selected polymers were measured in dimethyl sulfoxide (DMSO) solution and showed absorption bands in the range 253-398 nm, due to n-p* and p-p* transition. The morphological properties of selected examples were tested by scanning electron microscope (SEM). Moreover, the electrical conductivities and the doping with iodine were tested.

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“…Some thermally prepared copoly(amino acid) (proteinoid) materials have been reported to form unique assemblies in aqueous solution. These proteinoid assemblies have been studied as protocellular models by Fox and other researchers [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20]. Films of these proteinoid materials have been investigated as potential drug delivery systems for controlled release purposes [21][22][23].…”

mentioning

confidence: 99%

Synthesis of Copoly(amino acids) as Potential Biomaterials by Diphenyl Phosphoryl Azide

Yang

Wang

Ottenbrite

1993

Journal of Bioactive and Compatible Polymers

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A convenient chemical synthesis of copoly(amino acids) as potential biomaterials is described. Direct copolycondensations of α-amino acids using diphenyl phosphoryl azide (DPPA) as condensation agent were carried out in the presence of triethylamine (TEA) as a base. The amino acids used were β-benzyl-L-aspartate (Asp.Bz), γ-benzyl-L-glutamate (Glu.Bz), L-phenylalanine (Phe), and O-benzyl-L-tyrosine (Tyr.OBz). Copoly(amino acids) with weightaverage molecular weights up to 28,000 were obtained in reasonable yields. Bimodal molecular weight distribution was observed in all the cases. Both the overall yield of the product and the yield of high molecular weight fraction are influenced by [DPPA]/[Monomer] and [TEA]/[Monomer] ratios. No significant solvent effect was observed.

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Compartmentalization in proteinoid microspheres

Cited by 29 publications

References 13 publications

Origins of the protein synthesis cycle

Origins of the protein synthesis cycle

New polymer syntheses part: 54 novel conducting polymers and copolymers based on 4‐Teriary butyl‐cyclohexanone moiety in the main chain

Synthesis of Copoly(amino acids) as Potential Biomaterials by Diphenyl Phosphoryl Azide

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