Antimicrobial Peptide AP00003

     
 

APD ID:

AP00003

 
 

Name/Class:

Hs-AFP1 (HsAFP1, H. sanguinea antifungal protein 1; defensins; 4S=S; UCSS1a; BBS; BBMm_lipid?; plants)

 
 

Source:

Heuchera sanguinea

 
 

Sequence:

DGVKLCDVPSGTWSGHCGSSSKCSQQCKDREHFAYGGACHYQFPSVKCFCKRQC

 
 

Length:

54

 
 

Net charge:

6

 
 

Hydrophobic residue%:

33%

 
 

Boman Index:

1.95 kcal/mol

 
 

3D Structure:

Bridge

 
 

SwissProt ID:

Reference ID: Ref  

 
 

Activity:

antifungal,

 
 

Additional info:

In medium A supplemented with 1 mM CaCl2 and 50 mM KCl, the peptide is active against fungi B. cinerea (IC50 6 ug/ml), C. sphaerospermum (IC50 1 ug/ml), F. culmorum (IC50 1 ug/ml), L. maculans (IC50 25 ug/ml), P. digitatum (IC50 1 ug/ml), T. viride (IC50 15 ug/ml), S. tritici (IC50 0.5 ug/ml), and V. albo-atrum (IC50 12 ug/ml) (FEBS Lett. 1995 Jul 17;368(2):257-62). Both non-germinated and germinated conidia of F. moniliforme were susceptible to these peptides. Overall, F. moniliforme was more susceptible than A. flavus to the peptide. The peptide bound strongly to chitin, mannan, galactocerebrosides, and sphingomyelin (Mycopathologia. 1998-1999;144:87-91). [35S]Hs-AFP1 also bound specifically and reversibly to microsomal membranes derived from N. crassa hyphae with a Kd of 27 nM and a Bmax of 102 pmol/mg protein. The similarity in Kd value between binding sites on hyphae and microsomes indicates that Hs-AFP1 binding sites reside on the plasma membrane. Rs-AFP2 itself was able to compete with [35S]Hs-AFP1. (J Biol Chem. 1997;272:32176-81). The orginal APD entry was replaced APD 26/7/2008; updated Jan2017 by GW.

 
       
 

Title:

Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.

 
 

Author:

Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF1995

 
 

Reference:

FEBS Lett. 1995 Jul 17;368(2):257-62. PubMed.

 
       

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