Folding control in cyclic peptides through N-methylation pattern selection: formation of antiparallel beta-sheet dimers, double reverse turns and supramolecular helices by 3alpha,gamma cyclic peptides |
| |
Authors: | Amorín Manuel Castedo Luis Granja Juan R |
| |
Institution: | Departamento de Química Orgánica, Laboratorios del CSIC, Facultad de Química, Universidad de Santiago, 15782 Santiago de Compostela, Spain. |
| |
Abstract: | Peptide foldamers constitute a growing class of nanomaterials with potential applications in a wide variety of chemical, medical and technological fields. Here we describe the preparation and structural characteristics of a new class of cyclic peptide foldamers (3alpha,gamma-CPs) that, depending on their backbone N-methylation patterns and the medium, can either remain as flat rings that dimerize through arrays of hydrogen bonds of antiparallel beta-sheet type, or can fold into twisted double reverse turns that, in the case of double gamma-turns, associate in nonpolar solvents to form helical supramolecular structures. A 3alpha,gamma-CP consists of a number of multiples of a repeat unit made up of four amino acid residues of alternating chirality: three corresponding to alpha-amino acids and one to a gamma-amino acid (a cis-3-aminocycloalkanecarboxylic acid). |
| |
Keywords: | beta sheets foldamers helical structures peptides self‐assembly |
本文献已被 PubMed 等数据库收录! |
|