First crystallographic signature of an acyclic peptide nanorod: molecular mechanism of nanorod formation by a self-assembled tetrapeptide

Debasish Haldar; Arijit Banerjee; Michael G B Drew; Apurba Kumar Das; Arindam Banerjee

doi:10.1039/b302472p

First crystallographic signature of an acyclic peptide nanorod: molecular mechanism of nanorod formation by a self-assembled tetrapeptide

Chem Commun (Camb). 2003 Jun 21:(12):1406-7. doi: 10.1039/b302472p.

Authors

Debasish Haldar¹, Arijit Banerjee, Michael G B Drew, Apurba Kumar Das, Arindam Banerjee

Affiliation

¹ Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India.

PMID: 12841264
DOI: 10.1039/b302472p

Abstract

A terminally protected acyclic tetrapeptide Boc-Aib-Val-Aib-beta-Ala-OMe 1 (Aib: alpha-aminoisobutyric acid, beta-Ala: beta-Alanine) self-assembles into a continuous hydrogen-bonded supramolecular helix with an average diameter of 10 A (1 nm) starting from a double bend molecular conformation in crystals and further self-assembly of this supramolecular architecture leads to the formation of polydisperse nanorods of diameters 10-40 nm.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallography, X-Ray
Hydrogen Bonding
Microscopy, Electron
Models, Molecular
Nanotechnology
Oligopeptides / chemistry*
Protein Conformation*
Protein Folding
Structure-Activity Relationship

Substances

Oligopeptides