Tachyplesin: Difference between revisions
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Of those 3 linear derivatives of TP-I, 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. | Of those 3 linear derivatives of TP-I, 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. | ||
TP-I undergoes a conformational change in the <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 the presence of LPS, than in the presence of water </scene>, making it more stable. | TP-I undergoes a conformational change in the <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 the presence of LPS, than in the presence of water</scene>, making it more stable. | ||
== A Cys Deleted Linear Analog == | == A Cys Deleted Linear Analog == | ||
