Tachyplesin
From Proteopedia
(Difference between revisions)
| Line 21: | Line 21: | ||
== Relevance == | == Relevance == | ||
== Mode of action == | == Mode of action == | ||
| - | TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. | + | TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. The binding of TPI to LPS neutralizes LPS, which is widely considered as endotoxin. In addition to LPS binding, footpriting analysis has revealed the binding of TPI to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TPI and DNA is contributed by secondary structure of the peptide which contains an antiparallel beta-sheet constrained by two disulfide bridges and connected by beta-turn. |
== Function == | == Function == | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 07:05, 29 December 2014
Introduction
| |||||||||||
References
- ↑ 1.0 1.1 Laederach A, Andreotti AH, Fulton DB. Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry. 2002 Oct 15;41(41):12359-68. PMID:12369825
- ↑ Kushibiki T, Kamiya M, Aizawa T, Kumaki Y, Kikukawa T, Mizuguchi M, Demura M, Kawabata SI, Kawano K. Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide. Biochim Biophys Acta. 2014 Jan 2;1844(3):527-534. doi:, 10.1016/j.bbapap.2013.12.017. PMID:24389234 doi:http://dx.doi.org/10.1016/j.bbapap.2013.12.017
Proteopedia Page Contributors and Editors (what is this?)
Shulamit Idzikowski, Janak Raj Joshi, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky
