Tachyplesin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The aminoacid sequence of the TPI is H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH₂ with <scene name='67/671725/Tachyplesin_i/1'> disulfide bonds </scene> between Cys³ and Cys¹⁶/Cys⁷ and Cys¹². Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | The aminoacid sequence of the TPI is H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH₂ with <scene name='67/671725/Tachyplesin_i/1'> disulfide bonds </scene> between Cys³ and Cys¹⁶/Cys⁷ and Cys¹². Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | ||
There are three linear derivatives: <scene name='1ma4'>TPY4 </scene>, TPF4 and TPA4. | There are three linear derivatives: <scene name='67/671725/1ma4/1'>TPY4</scene>, TPF4 and TPA4. | ||
Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | ||
TPI undergoes confirmation change in presence of LPS. The backbone of the polypeptide becomes more rigid and twisted in presence of LPS, making it more stable. | TPI undergoes confirmation change in presence of LPS. The backbone of the polypeptide becomes more rigid and twisted in presence of LPS, making it more stable. | ||
