Accessibility navigation


Salts responsive nanovesicles through π-stacking induced self-assembly of backbone modified tripeptides

Koley, P., Drew, M. G. B. and Pramanik, A. (2011) Salts responsive nanovesicles through π-stacking induced self-assembly of backbone modified tripeptides. Journal of Nanoscience and Nanotechnology, 11 (8). pp. 6747-6756. ISSN 1533-4880

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1166/jnn.2011.4219

Abstract/Summary

A set of backbone modified peptides of general formula Boc-Xx-m-ABA-Yy-OMe where m-ABA is meta-aminobenzoic acid and Xx and Yy are natural amino acids such as Phe, Gly, Pro, Leu, Ile, Tyr and Trp etc., are found to self-assemble into soft nanovesicular structures in methanol-water solution (9:1 by v/v). At higher concentration the peptides generate larger vesicles which are formed through fusion of smaller vesicles. The formation of vesicles has been facilitated through the participation of various noncovalent interactions such as aromatic pi-stacking, hydrogen bonding and hydrophobic interactions. Model study indicates that the pi-stacking induced self-assembly, mediated by m-ABA is essential for well structured vesicles formation. The presence of conformationally rigid m-ABA in the backbone of the peptides also helps to form vesicular structures by restricting the conformational entropy. The vesicular structures get disrupted in presence of various salts such as KCl, CaCl(2), N(n-Bu)(4)Br and (NH(4))(2)SO(4) in methanol-water solution. Fluorescence microscopy and UV studies reveal that the soft nanovesicles encapsulate organic dye molecules such as Rhodamine B and Acridine Orange which could be released through salts induced disruption of vesicles.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:30429
Uncontrolled Keywords:Nanovesicles; peptides; self-assembly; responsive
Publisher:American Scientific Publishers

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation