Formation versus Hydrolysis of the Peptide Bond from a Quantum-mechanical Viewpoint : the Role of Mineral Surfaces and Implications for the Origin of Life
Rimola, Albert (Università di Torino. Dipartimento di Chimica IFM)
Ugliengo, Piero (Università di Torino. Dipartimento di Chimica IFM)
Sodupe Roure, Mariona (Universitat Autònoma de Barcelona. Departament de Química)

Fecha:	2009
Resumen:	The condensation (polymerization by water elimination) of molecular Building blocks to yield the first active biopolymers (e. g. of amino acids to form peptides) during primitive Earth is an intriguing question that nowadays still remains open since these processes are thermodynamically disfavoured in highly dilute water solutions. In the present contribution, formation and hydrolysis of glycine oligopeptides occurring on a cluster model of sanidine feldspar (001) surface have been simulated by quantum mechanical methods. Results indicate that the catalytic interplay between Lewis and Brønsted sites both present at the sanidine surface, in cooperation with the London forces acting between the biomolecules and the inorganic surface, plays a crucial role to: i) favour the condensation of glycine to yield oligopeptides as reaction products; ii) inhibit the hydrolysis of the newly formed oligopeptides. Both facts suggest that mineral surfaces may have helped in catalyzing, stabilizing and protecting from hydration the oligopeptides formed in the prebiotic era.
Derechos:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Lengua:	Anglès
Documento:	Article ; recerca ; Versió publicada
Materia:	Peptide bond formation ; Peptide hydrolysis ; Catalysis ; Mineral surfaces ; Theoretical calculations ; Prebiotic chemistry
Publicado en:	International journal of molecular sciences, Vol. 10 Núm. 3 (february 2009) , p. 746-760, ISSN 1422-0067

DOI: 10.3390/ijms10030746
PMID: 19399219

15 p, 650.6 KB

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