Synthesis of protected oligo(γ-methyl-L-glutamates) and study of their conformation in solution and at the air water interface

SCOPUS: NotDefined.jFLWNAinfo:eu-repo/semantics/publishe

reactivity of UNCAs with Grignard reagents

International audienc

synthesis of N-protected gamma-amino-beta-keto-esters from urethane N-carboxyanhydrides (UNCAs)

International audienc

Studies of the dimensions of oligopeptides by singlet-singlet energy transfer and theoretical calculations. I. Influence of glycine on the dimensions of tetrapeptides

The efficiency of energy transfer between a fluorescent donor, L-tyrosine, and a fluorescent acceptor, L-tryptophan, has been determined in R′-L-Trp-L-Ala-L-Tyr-R″, R′-L-Trp-L-Ala-L-Ala-L-Tyr-R″, and R′-L-Trp-Gly-L-Ala-L-Tyr-R″ in ethanol solution. The protecting groups R′ and R″ were respectively tert-butyloxycarbonyl and methyl ester. A conformational theoretical analysis of molecules studied has been performed in parallel on the basis of semiempirical conformational potential energy functions. In the theoretical models all the side chains have been represented by a methyl group. From the distribution of distances between chromophores obtained theoretically, transfer efficiencies have been computed assuming a random orientation of the chromophores (κ 2 = 2/3). The comparison of calculated efficiencies with the values determined experimentally for the same value of κ 2 has been used as a check for the theoretical model. Both experimental and theoretical studies have shown that the glycyl residue produces a reduction of dimensions when it replaces in a tetrapeptide a residue with a β-carbon atom such as the L-alanyl residue. However, only a qualitative agreement between experimental and theoretical values of the efficiencies has been obtained.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

diastereoselective synthesis of N-protected beta-amino-alpha-hydroxyacids (norstatines) from urethane N-carbobyanhydrides (UNCAs)

International audienc

Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39

peer reviewe

Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39

peer reviewe