Conformation of the Cecropin-Melittin Hybrid, Cecropin A(1-8)-Melittin (1-18) Antibacterial Peptide

Title: Conformation of the Cecropin-Melittin Hybrid, Cecropin A(1-8)-Melittin (1-18) Antibacterial Peptide

Volume: 11 Issue: 2

Author(s): Savita Tauro, Evans Coutinho and Sudha Srivastava

Affiliation:

Keywords: antibacterial peptide,, cecropin-melittin hybrid,, NMR,

Abstract: Cecropin A (1-8)-Melittin (1-18) is a synthetic cecropin A-melittin hybrid peptide with leishmanicidal activity. The primary sequence of the peptide is as follows: KWKLPKKIGIGAVLKVLTTGLPALIS-NH2. 1H and 13C 2D NMR techniques were used to deduce the conformational parameters of chemical shift, 3JNHα coupling constants, temperature coefficients of NH chemical shifts and the pattern of intra and inter-residue nOes. NMR studies were carried out in water (pH 6.0) and hexafluoroacetone (HFA). The peptide was found in a β-pleated structure in water, and in HFA it adopts a right-handed α-helix conformation. Solution structures generated using restrained molecular dynamics simulations were refined by Mardigras to R factors ranging from 0.5 to 0.6.

Cite this article as:

Tauro Savita, Coutinho Evans and Srivastava Sudha, Conformation of the Cecropin-Melittin Hybrid, Cecropin A(1-8)-Melittin (1-18) Antibacterial Peptide, Protein & Peptide Letters 2004; 11 (2) . https://dx.doi.org/10.2174/0929866043478347