Kinetic analysis of artificial peptide self-replication. Part I: the homochiral case.
Computational kinetic analysis of a lately discovered homochiral peptide self-replicator is presented. A 6-step kinetic model was designed that addresses the main reactions and hydrophobic interactions involved in this template-directed, autocatalytic system and that gave rise to excellent fitting of 4 previously published independent experimental series. The model sheds light on the mechanistic principle of the reaction system and illustrates directly a number of dynamic properties such as the observed autocatalytic efficiency. It was found that the dynamics are basically governed by two reversible hydrophobic interactions: between the template and a peptide fragment and between two template species. The later association was determined to be considerably more favored, which leads to the predominant presence of the catalytically inactive template dimer in the reaction system. Our results show that the involvement of a template trimer is not necessary to obtain the observed fittings.
Centro de Investigaciones Químicas, Universidad Autónoma del Estado de Morelos, Av. Universidad No 1001, Col. Chamilpa, 62210 Cuernavaca, Morelos, Mexico.
Jesús Rivera
JR
Islas
Véronique
V
Pimienta
Jean-Claude
JC
Micheau
Thomas
T
Buhse
D000465:Algorithms; D002384:Catalysis; D019281:Dimerization; D019418:Evolution, Chemical; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008956:Models, Chemical; D009716:Numerical Analysis, Computer-Assisted; D000069497:Origin of Life; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D013237:Stereoisomerism
D010446:Peptide Fragments; D010455:Peptides