Tachyplesin

(TPI) is an antimicrobial polypeptide originally detected in Japanese Horse Shoe Crab. It shows high affinity for lipopolysaccharides (LPS) of gram-negative bacteria, thus neutralizing its effects. It has also been reported to inhibit the growth of gram positive bacteria, fungui and viruses.

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 disulfide bonds 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. 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.

Importance

Relevance

Function

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