Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10536931 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2014 | 8 Pages |
Abstract
CD and NMR measurements revealed that binding to LPS slightly extends the two β-strands of TP I and stabilizes the whole structure of TP I. The fluorescence wavelength of an intrinsic tryptophan of TP I and fluorescence quenching in the presence or absence of LPS indicated that a tryptophan residue is incorporated into the hydrophobic environment of LPS. Finally, we succeeded in proposing a structural model for the complex of TP I and LPS by using a docking program. The calculated model structure suggested that the cationic residues of TP I interact with phosphate groups and saccharides of LPS, whereas hydrophobic residues interact with the acyl chains of LPS.
Keywords
Tachyplesin ILPSTOF MSTOCSYAMPsRMSDDPCnuclear magnetic resonanceroot-mean-square deviationNMRDodecylphosphocholinecircular dichroismTotal correlation spectroscopylipopolysaccharidematrix assisted laser desorption ionizationMALDIAntimicrobial peptideAntimicrobial peptideshigh performance liquid chromatographyHPLC
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Takahiro Kushibiki, Masakatsu Kamiya, Tomoyasu Aizawa, Yasuhiro Kumaki, Takashi Kikukawa, Mineyuki Mizuguchi, Makoto Demura, Shun-ichiro Kawabata, Keiichi Kawano,