Solid phase peptide synthesis and TLR-5 activity analysis of pertide fragments from the Salmonella muenchen flagellin protein

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Title: Solid phase peptide synthesis and TLR-5 activity analysis of pertide fragments from the Salmonella muenchen flagellin protein
Author: Joseph Richard Karam
Abstract: Drug design strategies begin by determining the simplest ligand necessary to activate a receptor of interest . The Toll -Like Receptor -5 (TLR -5 ) is an attractive target for pharmaceutical modulation because it initiates an innate immune response . A TLR -5 agonist or antagonist could help remedy a variety of disorders . Flagellin , the primary component of bacterial flagella , is the only known TLR -5 ligand . Three short regions within this protein are suggested to activate TLR -5 : Peptide -N1 , LQRVRELAVQ ; Peptide -N2 , LAVQSANGTNSQSD ; and Peptide -C1 , QNRFNSAITNLGNT . Here , we report the synthesis of these peptides and their activity against TLR -5 expressing HEK -293 cells . Our goal was to resolve the minimal region of flagellin necessary to bind and /or activate TLR -5 . Results showed significant agonist activity (P <0 .01 ) with peptide N2 -b (LAVQSANGTN ) , and peptide N2 -f (LAVQSANGTNSQ ) . Peptide N2 -c (ANGTN ) and N2 -d (LAVQS ) showed significant (P <0 .05 ) antagonistic properties for TLR -5 . These peptides could make interesting lead compounds to modify for optimal TLR -5 activity .
URI: http : / /hdl .handle .net /2152 .3 /215
Date: 2005-08-18

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Solid phase peptide synthesis and TLR-5 activity analysis of pertide fragments from the Salmonella muenchen flagellin protein. The University of Texas Medical Branch. Available electronically from http : / /hdl .handle .net /2152 .3 /215 .

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