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Protein Science (2007), 16:309-315. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Design of a functionally equivalent nonglycosylated analog of the glycopeptide antibiotic formaecin I

Kanwal J. Kaur, Shashank Pandey, and Dinakar M. Salunke

Structural Biology Unit, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India

(RECEIVED September 25, 2006; FINAL REVISION November 11, 2006; ACCEPTED November 12, 2006)

Various nonglycosylated analogs were designed in order to explore the role of glycosylation in formaecin I, an antibacterial glycopeptide of insect origin. The functional behavior of a designed nonglycosylated analog (P7,endo P8a,{Delta}T11)formaecin I was found to be similar to that of native glycosylated peptide. Both the peptides showed similar antibacterial activities against Escherichia coli and Salmonella strains. The designed nonglycosylated analog (P7,endo P8a,{Delta}T11)formaecin I has low binding affinity to LPS identical to that of native glycopeptide, formaecin I. Both the peptides have similar killing kinetics and are nontoxic to erythrocytes. Formaecin I and designed nonglycosylated (P7,endo P8a,{Delta}T11)formaecin I have no definite conformational features associated with them. The glycosylated residue of threonine in formaecin I and proline residues in designed peptide [(P7,endo P8a,{Delta}T11)formaecin I], possibly help in stabilizing the correct conformation that facilitates presentation of the peptide to its receptor. It is evident that a functionally equivalent nonglycosylated analog of native glycosylated antibacterial peptide can be designed by strategically modifying the sequence.

Keywords: glycopeptide antibiotic; rational design; antibacterial activity; insect immunity


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