Small and easy-to-do mimetics of beta-turns are of great interest to interfere with protein-protein recognition events mediated by beta-turn recognition motifs. We propose a straightforward procedure for constraining the conformation of tetrapeptides lacking a pre-formed scaffold. According to the stereochemistry array, N-Ts tetrapeptides including Thr or PhSer (phenylserine) at the positions 2 or 3 gave rise in a single step to the sequences Oxd(2)-Oxd(3) or Delta Abu(2)-Oxd(3) (Oxd, oxazolidin-2-one; Delta Abu, 2,3-dehydro-2-aminobutyric). These pseudo-Pro residues displayed highly constrained phi, psi, and chi dihedral angles, and induced clear beta-turns or inverse turns of type I or II, as determined by extensive spectroscopic and computational analyses
De Marco R, Greco A, Rupiani S, Tolomelli A, Tomasini C, Pieraccini S, et al. (2013). In-peptide synthesis of di-oxazolidinone and dehydroamino acid-oxazolidinone motifs as β-turn inducers. ORGANIC & BIOMOLECULAR CHEMISTRY, 11(26), 4316-4326 [10.1039/C3OB40357B].
In-peptide synthesis of di-oxazolidinone and dehydroamino acid-oxazolidinone motifs as β-turn inducers
DE MARCO, ROSSELLA;GRECO, ARIANNA;RUPIANI, SEBASTIANO;TOLOMELLI, ALESSANDRA;TOMASINI, CLAUDIA;PIERACCINI, SILVIA;GENTILUCCI, LUCA
2013
Abstract
Small and easy-to-do mimetics of beta-turns are of great interest to interfere with protein-protein recognition events mediated by beta-turn recognition motifs. We propose a straightforward procedure for constraining the conformation of tetrapeptides lacking a pre-formed scaffold. According to the stereochemistry array, N-Ts tetrapeptides including Thr or PhSer (phenylserine) at the positions 2 or 3 gave rise in a single step to the sequences Oxd(2)-Oxd(3) or Delta Abu(2)-Oxd(3) (Oxd, oxazolidin-2-one; Delta Abu, 2,3-dehydro-2-aminobutyric). These pseudo-Pro residues displayed highly constrained phi, psi, and chi dihedral angles, and induced clear beta-turns or inverse turns of type I or II, as determined by extensive spectroscopic and computational analysesI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
