Studies on the aggregation and possible channel formation in membranes of a cyclic hexapeptide, cyclo (D-Ala-L-Pro-L-Ala)2

Ramesh, J. ; Ghosh, J. K. ; Swaminathan, C. P. ; Ramasamy, P. ; Surolia, A. ; Sikdar, S. K. ; Easwaran, K. R. K. (2003) Studies on the aggregation and possible channel formation in membranes of a cyclic hexapeptide, cyclo (D-Ala-L-Pro-L-Ala)2 The Journal of Peptide Research, 61 (2). pp. 63-70. ISSN 1397-002X

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Official URL: http://onlinelibrary.wiley.com/doi/10.1034/j.1399-...

Related URL: http://dx.doi.org/10.1034/j.1399-3011.2003.00033.x

Abstract

The interaction of zwitterionic lipid DMPC and DPPC with cyclic hexapeptide, cyclo (d-Ala-l-Pro-l-Ala)2 was studied using circular dichroism (CD) and differential scanning calorimetry (DSC). Preliminary membrane conductance results showed that the peptide has a tendency to form channels inside the lipid bilayer. CD studies indicated that as the lipid/peptide (L/P) ratio (DMPC/peptide) was increased, the magnitude of the negative CD band having a λmax around 200 nm decreased. At a L/P ratio of 210:1, this band disappeared completely, indicating dramatic conformational changes in the peptide on interaction with the lipid bilayer. Reduction of the phase transition temperature and the maximum heat capacity of the lipid bilayer (DPPC) for gel-to-liquid crystalline phase transition indicates a strong interaction of the peptide with the lipid bilayer.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:BLM; CD; Channel; Cyclic Peptide; DSC; Lipid
ID Code:11120
Deposited On:09 Nov 2010 03:56
Last Modified:03 May 2012 05:16

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