Amyloid Aggregates Arise from Amino Acid Condensations under Prebiotic Conditions. (11th August 2016)

• Record Type: Journal Article
• Authors: Greenwald, Jason; Friedmann, Michael P.; Riek, Roland
• Is Part Of: Angewandte Chemie. Volume 128:Number 38(2016)
• Page Start: 11781
• Page End: 11785
• Publication Date: 2016-08-11
• Subjects: Aggregation -- Amyloide -- Peptide -- Präbiotische Chemie -- Selbstorganisation; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201605321
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: 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.