Self-assembled surfactant cyclic peptide nanostructures as stabilizing agents

Dindyal Mandal, Rakesh K. Tiwari, Amir Nasrolahi Shirazi, Donghoon Oh, Guofeng Ye, Antara Banerjee, Arpita Yadav, Keykavous Parang

Research output: Contribution to journalArticlepeer-review

Abstract

A number of cyclic peptides including [FR]4, [FK]4, [WK]5, [CR]4, [AK]4, and [WR]n (n = 3-5) containing l-amino acids were produced using solid-phase peptide synthesis. We hypothesized that an optimal balance of hydrophobicity and charge could generate self-assembled nanostructures in aqueous solution by intramolecular and/or intermolecular interactions. Among all the designed peptides, [WR] n (n = 3-5) generated self-assembled vesicle-like nanostructures at room temperature as shown by transmission electron microscopy (TEM), scanning electron microscopy (SEM), and/or dynamic light scattering (DLS). This class of peptides represents the first report of surfactant-like cyclic peptides that self-assemble into nanostructures. A plausible mechanistic insight into the self-assembly of [WR]5 was obtained by molecular modeling studies. Modified [WR]5 analogues, such as [WMeR]5, [WR(Me)2]5, [WMeR(Me)2]5, and [WdR]5, exhibited different morphologies to [WR]5 as shown by TEM observations. [WR]5 exhibited a significant stabilizing effect for generated silver nanoparticles and glyceraldehyde-3-phosphate dehydrogenase activity. These studies established a new class of surfactant-like cyclic peptides that self-assembled into nanostructures and could have potential applications for the stabilization of silver nanoparticles and protein biomolecules.

Original languageEnglish (US)
Pages (from-to)9465-9475
Number of pages11
JournalSoft Matter
Volume9
Issue number39
DOIs
StatePublished - Oct 21 2013
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Condensed Matter Physics

Fingerprint

Dive into the research topics of 'Self-assembled surfactant cyclic peptide nanostructures as stabilizing agents'. Together they form a unique fingerprint.

Cite this