Tachyplesin: Difference between revisions
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Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | ||
Along with TPI, there exists three linear derivatives: <scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4 as shown below. | |||
[[Image:derivatives.jpg]] | [[Image:derivatives.jpg]] | ||
Of those 3 linear derivatives of TPI, TPA4 was inactive which was due to its incapability to form hairpin loop structure. This guided to the conclusion that linear tachyplesin analogues do not show preferential affinity for LPS. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | |||
TPI undergoes confirmation change in <scene name='67/671725/Tp_i_in_the_presence_of_lps/1'>presence of LPS </scene>. The backbone of the polypeptide becomes <scene name='67/671725/Conformation_change/5'>more rigid and twisted in presence of LPS, than in the presence of water </scene>, making it more stable. | TPI undergoes confirmation change in <scene name='67/671725/Tp_i_in_the_presence_of_lps/1'>presence of LPS </scene>. The backbone of the polypeptide becomes <scene name='67/671725/Conformation_change/5'>more rigid and twisted in presence of LPS, than in the presence of water </scene>, making it more stable. | ||
