Antimicrobial Peptide AP00505

     
 

APD ID:

AP00505

 
 

Name/Class:

human Histatin 5 (hst5; primates, mammals, animals; His-rich; ZZHs; BBII; derivatives: Dh-5; Dhvar5; Dhvar4; demegen P-113; P113; Clinical)

 
 

Source:

Homo sapiens

 
 

Sequence:

DSHAKRHHGYKRKFHEKHHSHRGY

 
 

Length:

24

 
 

Net charge:

12

 
 

Hydrophobic residue%:

8%

 
 

Boman Index:

4.81 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

NMR

 
 

SwissProt ID:

SwissProt ID: P15516  Go to SwissProt

 
 

Activity:

anti-Gram+ & Gram-, antiviral, antifungal, anti-HIV, Surface immobilized AMPs, Anti-MRSA, Enzyme inhibitor,

 
 

Crucial residues:

Zn2+ binding is essential for antibacterial activity (FEBS Lett 2006; 273: 2399-2406).

 
 

Additional info:

Active against C. albicans. Also killing ESKAPE pathogens, such as S. aureus, P. aeruginosa and A. baumannii, E. cloacae, and E. faecium (Du H et al., 2017). Histatin 5 is a proteolytic product of histatin 3. The active domain of histitin 5 (Dh-5) corresponding to residues 11-24 showed HIV inhibitory effects. However,the results with the Dh-5 mutants are mixed (Groot et al. 2006 J. Virol. 80: 9236-9243). The sequence of Dhvar4 is KRLFKKLLFSLRKY, a helical peptide which is active against bacteria and fungi. Dhvar5 has a sequence LLLFLLKKRKKRKY, which is active against bacteria and fungi (Ruissen AL et al 2002 Peptides 23:1391-9). P-113 (P113) is a 12-residue active peptide corresponding to residues 4-15 of histatin 5 (Rothstein DM et al. 2001 AAC 45: 1367). Both the D and L forms (D=L) were equally active against C. albicans, but only the D-form (P113-D) was active in vivo (Sajjan US et al 2001 Antimicrob Agents Chemother 45:3437-3444). The His-His sequence is a good ligand for Cu2+ (Kulon K et al. 2008 J Inorg Biochem 102: 960-72). Enzyme inhibitor: Hst 5 is a competitive cysteine proteinase inhibitor (Gusman H et al., 2001). Derivatives were subjected to clinical trials. Dhvar5 has been covalently immobilized 2015 to chitosan film at 2 ng/cm2 and can decrease MRSA (MIC 0.5 ug/ml) colonization: adhesion (Costa FM et al. 2015). UPdated 6/2016; 4/2017.

 
       
 

Title:

Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.

 
 

Author:

Raj PA, Marcus E, Sukumaran DK, Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, Troxler RF.1988

 
 

Reference:

J Biol Chem. 1988 Jun 5;263(16):7472-7.

 
       

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