Lee D H, Granja J R, Martinez J A, Severin K, Ghadiri M R
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.
Nature. 1996 Aug 8;382(6591):525-8. doi: 10.1038/382525a0.
The production of amino acids and their condensation to polypeptides under plausibly prebiotic conditions have long been known. But despite the central importance of molecular self-replication in the origin of life, the feasibility of peptide self-replication has not been established experimentally. Here we report an example of a self-replicating peptide. We show that a 32-residue alpha-helical peptide based on the leucine-zipper domain of the yeast transcription factor GCN4 can act autocatalytically in templating its own synthesis by accelerating the thioester-promoted amide-bond condensation of 15- and 17-residue fragments in neutral, dilute aqueous solutions. The self-replication process displays parabolic growth pattern with the initial rates of product formation correlating with the square-foot of initial template concentration.
在似是而非的益生元条件下氨基酸的产生及其缩合形成多肽早已为人所知。但尽管分子自我复制在生命起源中至关重要，肽自我复制的可行性尚未通过实验得到证实。在此，我们报告一个自我复制肽的实例。我们表明，基于酵母转录因子GCN4亮氨酸拉链结构域的一个32个残基的α-螺旋肽，在中性、稀水溶液中，通过加速15个和17个残基片段的硫酯促进的酰胺键缩合，能够以自催化方式模板化自身的合成。自我复制过程呈现抛物线式增长模式，产物形成的初始速率与初始模板浓度的平方根相关。
