http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17347

Polyamino acids as synthetic enzymes: mechanism, applications and relevance to prebiotic catalysis (Articolo in rivista)

Type

Label

Polyamino acids as synthetic enzymes: mechanism, applications and relevance to prebiotic catalysis (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Carrea G., Colonna S., Kelly D.R., Lazcano A., Ottolina G., Roberts S.M. (2005)
Polyamino acids as synthetic enzymes: mechanism, applications and relevance to prebiotic catalysis
in Trends in biotechnology (Regul. ed.); Elsevier Science London, London (Regno Unito)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Carrea G., Colonna S., Kelly D.R., Lazcano A., Ottolina G., Roberts S.M. (literal)

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Istituto di Chimica del Riconoscimento Molecolare, CNR, Via Mario Bianco 9, 20131 Milano, Italy Istituto di Chimica Organica Alessandro Marchesini, Facoltà di Farmacia, via Venezian 21, 20133 Milano, Italy School of Chemistry, Cardiff University, PO Box 912, Cardiff, UK, CF10 2AT Facultad de Ciencias, UNAM, Apdo Postal 70-407, Cd.Universitaria, 04510 D.F., Mexico School of Chemistry, University of Manchester, Sackville Street, Manchester, UK, M60 1QD (literal)

Titolo

Polyamino acids as synthetic enzymes: mechanism, applications and relevance to prebiotic catalysis (literal)

Abstract

Polyamino acids, such as polyleucine, behave as synthetic enzymes in the asymmetric epoxidation of chalcone and other electron-deficient alkenes (the Julia-Colonna reaction). The influences of reaction conditions, of the molecular structure of the catalysts and of the scaling-up of the process on the enantioselectivity of the reaction have been determined. The kinetics and mechanism have been investigated using a soluble PEG-polyleucine conjugate, which behaves in a similar way to an enzyme, showing saturation kinetics for both chalcone and HOO-. Enantioselective catalysis is achieved with peptides with as few as five residues and scalemic catalysts show high chiral amplification. Here, we discuss the relevance of these-enzyme like catalysts to prebiotic processes, such as the role of small peptides in the formation of optically active cyanohydrins. (literal)

Editore