Effects Of Two Glycine Residues In Positions 13 And 17 Of Pleurocidin On Structure And Bacterial Cell Selectivity

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Abstract:

Pleurocidin (Ple), a 25-residue α-helical antimicrobial peptide, isolated from skin mucosa of the winter flounder, shows potent bacterial cell selectivity. In this study, the effect of two glycine residues in positions 13 and 17 of Ple on structure and bacterial cell selectivity was investigated by Gly┬«Ala substitution. Ala-substitution (Gly13, 17→Ala, Gly13→ Ala and Gly17→ Ala) in positions 13 and 17 of Ple did not induce a significant change in antibacterial activity, but increased hemolytic activity. Both Gly13→ Ala and Gly17→ Ala substitution did not cause a remarkable change in α-helical content in SDS micelles, while Gly13,17→Ala substitution caused a drastic increase in α-helical content. These results suggest that the hinge region from Gly13 to Gly17 of Ple is assumed to provide its conformational flexibility and bacterial cell selectivity.

Keywords: ala substitution; bacterial cell selectivity; pleurocidin; structure

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866043478383

Affiliations: Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University, Kwangju 501-759, Korea

Publication date: February 1, 2004

More about this publication?
  • 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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