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Biopanning of endotoxin-specific phage displayed peptides

Thomas, Celestine J and Sharma, Shilpi and Kumar, Gyanendra and Visweswariah, Sandhya S and Surolia, Avadhesha (2003) Biopanning of endotoxin-specific phage displayed peptides. In: Biochemical and Biophysical Research Communications, 307 (1). pp. 133-138.

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Abstract

Systemic bacterial infections frequently lead to a plethora of symptoms termed “endotoxic shock” or “sepsis.” Characterized by hypotension, coagulation abnormalities, and multiple organ failure, treatment of sepsis still remains mostly supportive. Of the various experimental therapeuticinterventional strategies, neutralization of endotoxin by peptides or proteins is becoming popular recently. Hence, design of endotoxin binding peptides is gaining currency as their structural complexity and mode of recognition of endotoxin precludes mounting of resistance against them by the susceptible bacteria by genetic recombination, mutation, etc. Earlier work from our laboratory had shown that the amphiphilicc ationic peptides are good ligands for endotoxin binding. In this study, we report the results of studies with the 12 selected lipid A binding phage displayed peptides by biopanning of a repertoire of a random pentadecapeptide library displayed on the .lamentous M-13 phage. A comparison of the sequences revealed no consensus sequence between the 12 selected peptides suggesting that the lipid A binding motif is not sequence speci.c which is in accord with the sequence variation seen with the naturally occurring anti-microbial and/or endotoxin binding peptides. Thus, the .exibility of the peptides coupled with their plasticity in recognizing the lipid A moiety, explains their tight binding to ndotoxin. At a structural level, asymmetric distribution of the charged polar residues on one face of the helix and non-polar residues on the opposite face appears to correlate with their activity.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Lipopolysaccharide;Lipid A;Endotoxin;Surface plasmon resonance;Biopanning.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)
Date Deposited: 03 Dec 2008 07:24
Last Modified: 19 Sep 2010 04:53
URI: http://eprints.iisc.ernet.in/id/eprint/16632

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