1031759-99-5Relevant academic research and scientific papers
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
Amorin, Manuel,Castedo, Luis,Granja, Juan R.
, p. 2100 - 2111 (2008)
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 examino acids and one to a γ-amino acid (a cis-3-aminocycloalkanecarboxylic acid).
