Chiral polymerization: symmetry breaking and entropy production in closed systems

We solve numerically a kinetic model of chiral polymerization in systems closed to matter and energy flow, paying special emphasis to its ability to amplify the small initial enantiomeric excesses due to the internal and unavoidable statistical fluctuations. The reaction steps are assumed to be reversible, implying a thermodynamic constraint among some of the rate constants. Absolute asymmetric synthesis is achieved in this scheme. The system can persist for long times in quasi- stationary chiral asymmetric states before racemizing. Strong inhibition leads to long-period chiral oscillations in the enantiomeric excesses of the longest homopolymer chains. We also calculate the entropy production {\sigma} per unit volume and show that {\sigma} increases to a peak value either before or in the vicinity of the chiral symmetry breaking transition

Amyloid Aggregates Arise from Amino Acid Condensations under Prebiotic Conditions

Current theories on the origin of life reveal significant gaps in our understanding of the mechanisms that allowed simple chemical precursors to coalesce into the complex polymers that are needed to sustain life. The volcanic gas carbonyl sulfide (COS) is known to catalyze the condensation of amino acids under aqueous conditions, but the reported di‐, tri‐, and tetra‐peptides are too short to support a regular tertiary structure. Here, we demonstrate that alanine and valine, two of the proteinogenic amino acids believed to have been among the most abundant on a prebiotic earth, can polymerize into peptides and subsequently assemble into ordered amyloid fibers comprising a cross‐β‐sheet quaternary structure following COS‐activated continuous polymerization of as little as 1 mm amino acid. Furthermore, this spontaneous assembly is not limited to pure amino acids, since mixtures of glycine, alanine, aspartate, and valine yield similar structures.Once upon a time: The aqueous synthesis of peptides under conditions that are relevant to a prebiotic earth leads to the formation of ordered amyloid aggregates. With mixtures of four amino acids, such conditions yield thousands of unique peptides that then undergo a spontaneous selection and self‐assembly process. The inherent ability of simple peptides to form ordered quaternary structures may be relevant to the origins of biological macromolecules.Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/137528/1/anie201605321_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/137528/2/anie201605321.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/137528/3/anie201605321-sup-0001-misc_information.pd

Oligopeptides and copeptides of homochiral sequence, via beta-sheets, from mixtures of racemic alpha-amino acids, in a one-pot reaction in water; relevance to biochirogenesis.

International audienceAs part of our studies on the biochirogenesis of peptides of homochiral sequence during early evolution, the formation of oligopeptides composed of 14-24 residues of the same handedness in the polymerization of dl-leucine (Leu), dl-phenylalanine (Phe), and dl-valine (Val) in aqueous solutions, by activation with N, N'-carbonyldiimidazole and then initiation with a primary amine, in a one-pot reaction, was demonstrated by MALDI-TOF MS using deuterium enantio-labeled alpha-amino acids. The formation of long isotactic peptides is rationalized by the following steps occurring in tandem: (i) creation of a library of short diasteroisomeric oligopeptides containing isotactic peptides in excess in comparison to a binomial kinetics, as a result of an asymmetric induction exerted by the N-terminal residue of a given handedness; (ii) precipitation of the less soluble racemic isotactic penta- and hexapeptides in the form of beta-sheets that are delineated by homochiral rims; (iii) regio-enantiospecific chain elongation occurring heterogeneously at the beta-sheets/solution interface. Polymerization of l-Leu with l-isoleucine (Ile) or l-Phe with l- (1) N-Me-histidine yielded mixtures of copeptides containing both residues. In contrast, in the polymerization of the corresponding mixtures of l- + d-alpha-amino acids, the long oligopeptides were composed mainly from oligo- l-Leu and oligo- d-Ile in the first system and oligo- d-Phe in the second. Furthermore, in the polymerization of mixtures of hydrophobic racemic alpha-amino acids dl-Leu, dl-Val, and dl-Phe and with added racemic dl-alanine and dl-tyrosine, copeptides of homochiral sequences are most dominantly represented. Possible routes for a spontaneous "mirror-symmetry breaking" process of the racemic mixtures of homochiral peptides are presented

N-Benzyl-5-(dimethylamino)naphthalene-1-sulfonamide

The structure of the title compound, C19H20N2O2S, displays intermolecular N—H...O hydrogen bonding, which generates inversion dimers. There is no π–π stacking in the crystal structure. The dihedral angle between the phenyl ring and naphthalene ring system is 59.16 (11)°