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Tachyplesin
From Proteopedia
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<StructureSection load='1MA2' size='340' side='right' caption='1MA2' scene=''> | <StructureSection load='1MA2' size='340' side='right' caption='1MA2' scene=''> | ||
Tachyplesin I (TPI) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It shows high affinity for [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects. It has also been reported to inhibit the growth of gram positive bacteria, fungui and viruses. | Tachyplesin I (TPI) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It shows high affinity for [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects. It has also been reported to inhibit the growth of gram positive bacteria, fungui and viruses. | ||
| + | <Structure load='1ma2' size='350' frame='true' align='right' caption='1ma2' scene='Insert optional scene name here' /> | ||
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| + | <scene name='60/607863/N_to_c_rainbow/1'>N to C sequence</scene> | ||
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| + | {{Template:ColorKey_Amino2CarboxyRainbow}} | ||
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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. 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. | 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. 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. | ||
Revision as of 13:52, 26 December 2014
Introduction
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References
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