Jump to content

User:Sagearbor/CTP test Subpage

From Wikipedia, the free encyclopedia

Definition

[edit]

Cyclic Tetrapeptides (CTPS) are a sequence of 4 amino acids usually cyclized through a amide bond between the N-terminus amide and C-terminus carboxyl, also known as "head to tail" cyclization.

Naturally occuring cyclic tetrapeptides

[edit]

A range of naturally occurring CTPs have been discovered which have plethora of biological activity. Table 1 describes some briefly.


Cyclic Tetrapeptide Description Structure
Tentoxin Produced by phytopathogenic fungus Alternaria alternata. It selectively induces chlorosis in several germinating seedling plants. Therefore, tentoxin may be used as a potential natural herbicide. (cyclo(N-methyl-L-alanyl-L-leucyl-N-methyl-trans-dehydrophenyl-alanyl-glycyl)) structure pic add later
HC-Toxin descrip structure pic add later
chlamydocin descrip structure pic add later
Cyl-1 descrip structure pic add later
Cyl-2 descrip structure pic add later
WF-3161 descrip structure pic add later
trapoxins A descrip structure pic add later
trapoxins B descrip structure pic add later
apicidin descrip structure pic add later




Propsed uses as protein reverse turn mimics

[edit]

Work by Arbor, Che, and Marshall has computationally probed CTPs as possible turn mimetics.[1][2]

Future work

[edit]

While several CTPs have been structurally described through NMR or X-ray crystallography a much larger set has been predicted computationally. Taking a predicted CTP conformation and modifying it to mimics a well known reverse turn and testing for structural similarity and binding affinity would be a significant next step in the use of CTPs as therapeutics.

See also

[edit]

Category:Reference

References

[edit]
  1. ^ A virtual library of constrained cyclic tetrapeptides that mimics all four side-chain orientations for over half the reverse turns in the protein data bank. Sage Arbor, Garland R. Marshall J Comput Aided Mol Des. 2009 February; 23(2): 87–95. Published online 2008 September 17. doi: 10.1007/s10822-008-9241-4
  2. ^ Biopolymers. 2008;90(3):384-93. c[D-pro-Pro-D-pro-N-methyl-Ala] adopts a rigid conformation that serves as a scaffold to mimic reverse-turns. Arbor S, Kao J, Wu Y, Marshall GR. Source Department of Biochemistry and Molecular Biophysics, Washington University, St. Louis, MO 63110, USA.