Antimicrobial Peptide AP00897

     
 

APD ID:

AP00897

 
 

Name/Class:

NA-CATH (N. atra cathelicidin; snake, reptiles, animals)

 
 

Source:

Naja atra

 
 

Sequence:

KRFKKFFKKLKNSVKKRAKKFFKKPKVIGVTFPF

 
 

Length:

34

 
 

Net charge:

15

 
 

Hydrophobic residue%:

38%

 
 

Boman Index:

2.03 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

NMR

 
 

SwissProt ID:

Reference ID: Ref  

 
 

Activity:

Anti-Gram+ & Gram-, Antibiofilm,

 
 

Crucial residues:

 
 

Additional info:

Discovered in 2008 (see the ref), this peptide is rich in lysines (38%). NA-CATH is predominantly alpha-helical in SDS and TFE (Dean S et al., 2011a). Active against Gram- and Gram+ bacteria (A. actinomycetemcomitans, E. coli, F. novicida, P. aeruginosa, B. thailandensis, and S. aureus) (Amer L et al., 2010;de Latour F et al., 2010; Dean S et al., 2011a;Dean S et al., 2011b) at concentrations < 1 ÁM). NA-CATH has low toxicity against host cells (de Latour F et al., 2010). It also has anti-biofilm activity against S. aureus (Dean S et al., 2011a). These studies also showed that small 11-aa peptide variants based on a repeated pattern within NA-CATH (KR(F/A)KKFFKK(L/P)K) have similar antimicrobial and anti-biofilm activity to the parent peptide, but not when proline is present (de Latour F et al., 2010; van Hoek M, 2014). NMR studies revealed a well-defined helical region between residues 3-23 with the rest 11 residues disordered in the micelle-bound state Du H et al., 2015. Updated and written by Monique L. van Hoek 5Jan2015; 2/2015; GW 7/2015.

 
       
 

Title:

Identification and characterization of novel reptile cathelicidins from elapid snakes.

 
 

Author:

Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y.2008

 
 

Reference:

Peptides. 2008 Oct;29(10):1685-1691. PubMed.

 
       

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