Assisted dipeptide bond formation: glycine as a case study

Achour, S., Hosni, Z., Darghouthi, S. and Syme, C. (2021) Assisted dipeptide bond formation: glycine as a case study. Heliyon, 7(6), e07276. (doi: 10.1016/j.heliyon.2021.e07276) (PMID:34195408) (PMCID:PMC8225972)

Abstract

Peptide bond formation is a crucial chemical process that dominates most biological mechanisms and is claimed to be a governing factor in the origin of life. Dipeptides made from glycine are studied computationally via Density Functional Theory (DFT) using two different basis sets. This reaction was investigated from both a thermodynamic and kinetic point of view. The effect of explicit assistance via the introduction of discrete solvent molecules was investigated. Water, methanol, and cyclohexane were all employed as solvent media in addition to gas to investigate their effects on the mechanism of peptide bond formation. This computational investigation revealed that methanol is slightly better than water to leverage peptide bond formation both kinetically and thermodynamically, while cyclohexane, a non-polar and non-protic solvent, is the least effective after gas as a medium of solvation. Energetic results in the gas environment are very close to those obtained in polar and protic solvents, suggesting that peptide bonds can be formed under interstellar conditions.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Syme, Dr Christopher
• Authors: Achour, S., Hosni, Z., Darghouthi, S., and Syme, C.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity
• Journal Name: Heliyon
• Publisher: Elsevier (Cell Press)
• ISSN: 2405-8440
• ISSN (Online): 2405-8440
• Published Online: 14 June 2021
• Copyright Holders: Copyright © 2021 Elsevier Ltd.
• First Published: First published in Heliyon 7(6): e07276
• Publisher Policy: Reproduced under a Creative Commons License