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

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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 nOe's. 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.

Keywords: NMR; antibacterial peptide; cecropin-melittin hybrid

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866043478347

Affiliations: Dept. of Pharmaceutical Chemistry, Bombay College of Pharmacy, Kalina, Mumbai 400 098, India.

Publication date: 2004-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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