Issue 40, 2017

The templation effect as a driving force for the self-assembly of hydrogen-bonded peptidic capsules in competitive media

Abstract

Peptide-based cavitands (resorcin[4]arenes substituted with histidine and glutamine hydrazides) exist as monomeric species in polar solvents (DMSO and methanol). Upon complexation of fullerenes, the cavitands wrap around the hydrophobic guests forming dimeric capsular shells (as evidenced by DOSY). The self-assembly of the cavitands is based on the formation of beta-sheet-like binding motifs around the hydrophobic core. In a polar environment, these hydrogen bonded structures are kinetically stable and highly ordered as manifested by a 100-fold increase of intensity of circular dichroism bands, as well as a separate set of signals and substantial differences in chemical shifts in NMR spectra. This behavior resembles a protein folding process at the molten globule stage with non-specific hydrophobic interactions creating a protective and favourable local environment for the formation of secondary structures of proteins.

Graphical abstract: The templation effect as a driving force for the self-assembly of hydrogen-bonded peptidic capsules in competitive media

Supplementary files

Article information

Article type
Paper
Submitted
02 Leq 2017
Accepted
24 Leq 2017
First published
01 Way 2017
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2017,15, 8513-8517

The templation effect as a driving force for the self-assembly of hydrogen-bonded peptidic capsules in competitive media

M. Grajda, M. J. Lewińska and A. Szumna, Org. Biomol. Chem., 2017, 15, 8513 DOI: 10.1039/C7OB01925D

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