Premium
Folding Control in Cyclic Peptides through N‐Methylation Pattern Selection: Formation of Antiparallel β‐Sheet Dimers, Double Reverse Turns and Supramolecular Helices by 3α,γ Cyclic Peptides
Author(s) -
Amorín Manuel,
Castedo Luis,
Granja Juan R.
Publication year - 2008
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200701059
Subject(s) - antiparallel (mathematics) , cyclic peptide , supramolecular chemistry , peptide , beta sheet , chemistry , chirality (physics) , folding (dsp implementation) , amino acid , hydrogen bond , stereochemistry , crystallography , molecule , organic chemistry , physics , crystal structure , biochemistry , nambu–jona lasinio model , chiral symmetry breaking , engineering , quantum mechanics , magnetic field , electrical engineering , quark
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 (3α,γ‐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 β‐sheet type, or can fold into twisted double reverse turns that, in the case of double γ‐turns, associate in nonpolar solvents to form helical supramolecular structures. A 3α,γ‐CP consists of a number of multiples of a repeat unit made up of four amino acid residues of alternating chirality: three corresponding to α‐amino acids and one to a γ‐amino acid (a cis ‐3‐aminocycloalkanecarboxylic acid).