Exploring structural features of folded peptide architectures in the construction of nanomaterials. Issue 61 (11th July 2016)

• Record Type: Journal Article
• Authors: Misra, Rajkumar; Reja, Rahi M.; Narendra, Lagumaddepalli V.; George, Gijo; Raghothama, Srinivasarao; Gopi, Hosahudya N.
• Is Part Of: Chemical communications. Volume 52:Issue 61(2016)
• Page Start: 9597
• Page End: 9600
• Publication Date: 2016-07-11
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c6cc04502b
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Supramolecular assemblies of conformationally biased α, γ-hybrid peptides composed of alternating α-Phe and 4, 4-dimethyl substituted γ-amino acids are investigated. Abstract : We are reporting the influence of foldamer structures on their self-assembled architectures. In a sharp contrast to the ordered α, γ-hybrid 12-helix obtained from 1 : 1 alternating Aib and γ-Phe, the α, γ-hybrid peptides constituted with α-Phe and 4, 4-dimethyl γ-amino acid (Aic) displayed the extended sheet type of conformations in solution and spontaneously self-assembled into thermally and proteolytically stable capsules. In contrast, the conformationally ordered 12-helix self-assembled into a three-dimensional supramolecular polyhedron.