Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine.

TitleTerminal is important for the helicity of the self-assemblies of dipeptides derived from alanine.
Publication TypeJournal Article
Year of Publication2013
AuthorsFu Y, Li B, Huang Z, Li Y, Yang Y
JournalLangmuir : the ACS journal of surfaces and colloids
Volume29
Issue20
Pagination6013-7
Date Published2013 May 21
Abstract

The organization of peptides and proteins attracts much attention, due to the biofunctionalities of the self-assemblies. Herein, four dipeptides derived from alanine were synthesized. It was found that the handedness of their self-assemblies was controlled by the chirality of the alanines at the terminals. The organic self-assemblies were studied using circular dichroism, (1)H NMR, Fourier transform infrared, field-emission electron microscopy, transmission electron microscopy, and X-ray diffraction. The results indicated that the electrostatic interactions among the carboxylate groups and H-bondings among the amide groups at the terminals play important roles in the formation of the organic self-assemblies.

DOI10.1039/c3an01929b
Alternate JournalLangmuir