Antimicrobial Peptide AP00339

     
 

APD ID:

AP00339

 
 

Name/Class:

Chrysophsin-1 (CHY1; madai, fish, animals; XXA; BBMm , UCLL1c)

 
 

Source:

the pyloric caeca and gills; Red sea bream, Chrysophrys major or Pagrus major

 
 

Sequence:

FFGWLIKGAIHAGKAIHGLIHRRRH

 
 

Length:

25

 
 

Net charge:

6

 
 

Hydrophobic residue%:

48%

 
 

Boman Index:

1.1 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

CD

 
 

SwissProt ID:

SwissProt ID: P83545  Go to SwissProt

 
 

Activity:

Anti-Gram+ & Gram-, Hemolytic, Anticancer

 
 

Crucial residues:

RRRH is critical for activity against Gram- E. coli (Fulmer et al., 2010).

 
 

Additional info:

Active against Gram+ L. garvieae YT-3(ATCC 49156) (MIC 10 uM), S. iniae F-8502 (MIC 2.5 uM), Gram- V. anguillarum ATCC 19264 (MIC 2.5 uM), Vibriopenaeicida KHA (MIC 10 uM), V. harveyi HUFP911 1 (ATCC 14126) (MIC 2.5 uM), V. vulnificus ET-7617(ATCC 33148) (MIC 5 uM), A. salmonicida NCMB 1102 (MIC 10 uM), and P. putida ATCC 12633 (MIC 40 uM). Covalent immobilization of the peptide via a flexible linker results in 82 11% of bacteria being killed by the AMP (Ivanov IE,et al 2012). It contains an unusual C-terminal RRRH sequence. The alpha-helical structure of this peptide is predicted and is confirmed by CD spectroscopy. It kills cancer cells by disrupting membranes (Hsu JC,et al 2011).

This peptide remains active against E. coli and S. aureus after surface immobilization and a flexible linker, as well as right lenght, is needed (Ivanov et al., 2012; Lozeau et al., 2015).

Found in multiple species. Updated 10/2012; 11/2015; Jan2017; 5/2017; 11/2018.

 
       
 

Title:

Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major.

 
 

Author:

Iijima N, Tanimoto N, Emoto Y, Morita Y, Uematsu K, Murakami T, Nakai T.2003

 
 

Reference:

Eur. J. Biochem. 2003; 270:675-686. PubMed.

 
       

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