Antimicrobial Peptide AP00366

     
 

APD ID:

AP00366

 
 

Name/Class:

BMAP-27 (BMAP27, bovine myeloid antimicrobial peptide 27; bovine cathelicidin, cattle, ruminant, mammals, animals; ZZHs; ZZP; UCLL1; Derivatives: BMAP-18 and BMAP-15)

 
 

Source:

Cow Bos taurus

 
 

Sequence:

GRFKRFRKKFKKLFKKLSPVIPLLHLG

 
 

Length:

27

 
 

Net charge:

10

 
 

Hydrophobic residue%:

40%

 
 

Boman Index:

1.64 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

NMR

 
 

SwissProt ID:

PDB ID: 2KET   Go to PDB

 
 

Activity:

Anti-Gram+ & Gram-, Antiviral, Antifungal, Antiparasitic, Anti-HIV, Anti-MRSA, Hemolytic, Antibiofilm, Anticancer

 
 

Additional info:

Active against E. coli, S. typhimurium, P. aeruginosa, S. marcescens, S. aureus (MRSA), S. epidermidis, B. megaterium (MIC 1-4 uM), C. albicans, and C. neoformans (MIC 4-8 uM). You can rotate, zoom, and view the 3D structure here in the PDB . The authors found that truncation of the C-terminal hydrophobic tail (BMAP27(1-18)) improved peptide selectivity but had little effect on antimicrobial activity. In addition, BMAP-18 ( i.e. N-terminal 18-residues of BMAP-27) is HIV-active. Further deletion of three C-terminal residues from BMAP-18 led to a peptide (BMAP-15) that is inactive to HIV-1 (Wang, G., et al. 2008. Antimicrobial Agents & Chemotherapy 52: 3438-3440). BMAP-18 has also been shown to Kill Trypanosomatid Parasites [PLoS Negl Trop Dis. 2009;3(2):e373]. BMAP-18 has been covalently linked to agarose beads or titanium surface with activity against S. epidermidis (Boix-Lemonche et al., 2019). Updated 2/2009; 10/2019.

 
       
 

Title:

Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities.

 
 

Author:

Skerlavaj B., Gennaro R., Bagella L., Merluzzi L, Risso A, Zanetti M.1996

 
 

Reference:

J. Biol. Chem. 1996; 271: 28375-28381. PubMed.

 
       

Close this window