Antimicrobial Peptide AP00008

     
 

APD ID:

AP00008

 
 

Name/Class:

Bactenecin (Cyclic dodecapeptide, bovine cathelicidin, cattle, ruminant, mammals; animals; BBMm; JJsn; 1S=S; Derivatives: Bac2A; IDR-1018)

 
 

Source:

Bovine neutrophils, Bos taurus

 
 

Sequence:

RLCRIVVIRVCR

 
 

Length:

12

 
 

Net charge:

4

 
 

Hydrophobic residue%:

66%

 
 

Boman Index:

2.52 kcal/mol

 
 

3D Structure:

Unknown

 
 

SwissProt ID:

SwissProt ID: P22226  Go to SwissProt

 
 

Activity:

anti-Gram+ & Gram-, wound healing,

 
 

Crucial residues:

The S-S bond, charged Arg and amidation

 
 

Additional info:

Active against B. megatherium Bml 1 (MIC 11 uM), B. subtilis Bs11 (MIC 17 uM), and M. luteus Mill (MIC 20 uM) (provided by Chunfeng Wang). A S-S bond led to a CYCLIC DODECAPEPTIDE, which is more active against gram- bacteria. Only linearized versions of the peptides (Bac2A, obtained by converting the two Cys residues to Ala residues, plus C-terminal amidation) showed activtiy against Gram+ bacteria such as S. epidermidis and E. facaelis. The linearized or reduced forms appeared to be more effective in dissipating the membrane potential (Wu M and Hancock,RE 1999 JBC 274: 29-35). Like NaD1, Bac2A is unable to disrupt SUVs and interacts with intracellular targets yet to be identified (van der Weerden et al. 2010 JBC 285:37513-20). This peptide displayed synergistic effects with indolicidin (entry 150) against E. coli (Yan H & Hancock REW 2001 Antimicrob Agents Chemother 45: 1558-60). IDR-1018 has wound healing capability. APD Updated Jan 2011; 4/2016; 9/2017.

 
       
 

Title:

Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils.

 
 

Author:

Romeo D, Skerlavaj B, Bolognesi M, Gennaro R.1988

 
 

Reference:

J Biol Chem. 1988 Jul 15;263(20):9573-5. PubMed.

 
       

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