Tachyplesin: Difference between revisions
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Among all the existing interactions, cysteine bridge being considered as the principal contributor of the structure, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below: | Among all the existing interactions, cysteine bridge being considered as the principal contributor of the structure, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below: | ||
[[Image: | [[Image:Seq TPI.jpg.jpg]] | ||
Of those 3 linear derivatives of TP-I, NMR structural investigation had shown TPA4 to be unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | Of those 3 linear derivatives of TP-I, NMR structural investigation had shown TPA4 to be unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | ||
