Issue 22, 2016

Supramolecular tryptophan-zipper forms a tripeptide as a regular proton transporter

Abstract

The diverse structure and assembly of two peptide analogues have been investigated. The tripeptide containing tryptophan, α-aminoisobutyric acid and valine self-assembles through various noncovalent interactions to form a tryptophan-zipper-like structure by intermolecular hydrogen bonding and π–π interactions. But the leucine analogue adopts a water-mediated hydrogen-bonded cage-like structure. X-ray crystallography shed some light on the structure of the tryptophan-zipper at the atomic level. Moreover, in U-tube experiments using pH gradient as the driving force across a liquid chloroform phase, the supramolecular tryptophan-zipper acts as a passive regular proton transporter.

Graphical abstract: Supramolecular tryptophan-zipper forms a tripeptide as a regular proton transporter

Supplementary files

Article information

Article type
Paper
Submitted
14 okt 2015
Accepted
08 jan 2016
First published
11 jan 2016

CrystEngComm, 2016,18, 4109-4114

Supramolecular tryptophan-zipper forms a tripeptide as a regular proton transporter

D. Podder, S. Sasmal, K. Maji and D. Haldar, CrystEngComm, 2016, 18, 4109 DOI: 10.1039/C5CE02005K

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