Antimicrobial Peptide AP00541

     
 

APD ID:

AP00541

 
 

Name/Class:

Polybia-MPI (Polybia-MP-I; insects, arthropods, invertebrates, animals, XXA; VIHNN; in vivo test)

 
 

Source:

venom, social wasp, Polybia paulista

 
 

Sequence:

IDWKKLLDAAKQIL

 
 

Length:

14

 
 

Net charge:

2

 
 

Hydrophobic residue%:

57%

 
 

Boman Index:

0.64 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

CD

 
 

SwissProt ID:

Reference ID: Ref  

 
 

Activity:

anti-Gram+ & Gram-, antifungal, Chemotactic, Cancer cells

 
 

Crucial residues:

helical structure

 
 

Additional info:

Active against E. coli (MIC 8 ug/ml), P. aeruginosa (MIC 8 ug/ml), B. subtilis (MIC 4 ug/ml), and S. aureus (MIC 15 ug/ml). Have anti-biofilm and antifungal activities against C. albicans and C. glabrata (Wang K et al. 2014). A mast cell lytic peptide, chemotaxis for polymorphonucleated leukocytes (PMNL). Not toxic to rat erythrocytes. Helix in SDS or TFE. Replacement of residue 7, 8, or 9 by a proline led to reduced helicity as well as antitumor activity (Wang et al. 2008) Peptides 29: 963-968. Animal model:mouse: A single atom change (CO-NH2 to CS-NH2) of MPI improved peptide stability to serum proteases and better inhibited sarcoma xenograft tumor (S180) growth from 18 (WT) to 38% (mutant) using a Kunming mouse model (Zhang W et al. 2010 Peptides 31:1832-8). Updated 9/6/12; 3/2014; Jan2017; GW.

 
       
 

Title:

Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista

 
 

Author:

Souza BM, Mendes MA, Santos LD, Marques MR, Cesar LM, Almeida RN, Pagnocca FC, Konno K, Palma MS2005

 
 

Reference:

Peptides. 2005 Nov;26(11):2157-64. Pub-Med.

 
       

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