2005
DOI: 10.1016/j.febslet.2005.03.046
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The hydrophobic surface of PaAMP from pokeweed seeds is essential to its interaction with fungal membrane lipids and the antifungal activity

Abstract: PaAMP is a small seed-specific antimicrobial protein from pokeweeds. It has a cysteine-knot fold with a positive patch and a hydrophobic surface. Site-specific mutagenesis was performed to study the roles of these two domains in antimicrobial activity and we found that the mutations in the hydrophobic surface had a more profound effect than that in the positive patch. A protein-membrane interaction was observed with the green fluorescence protein-PaAMP (GFP-AMP) fusion protein. The mutations that replace the a… Show more

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Cited by 7 publications
(6 citation statements)
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“…For relationship between structure and activity, linearization of cyclic antimicrobial peptides generally alters their activities as well as their ability to interact with cell membranes28–33. Furthermore, Peng et al reported that the positive patch and the hydrophobic surface were both important for the antifungal function of Pa ‐AMP from poke weed ( P. americana ) seeds34. Most of antimicrobial peptides with chitin‐binding capability were classified into knottin type or hevein type.…”
Section: Discussionmentioning
confidence: 99%
“…For relationship between structure and activity, linearization of cyclic antimicrobial peptides generally alters their activities as well as their ability to interact with cell membranes28–33. Furthermore, Peng et al reported that the positive patch and the hydrophobic surface were both important for the antifungal function of Pa ‐AMP from poke weed ( P. americana ) seeds34. Most of antimicrobial peptides with chitin‐binding capability were classified into knottin type or hevein type.…”
Section: Discussionmentioning
confidence: 99%
“…Another study showed the relationship between the hydrophobic character of a small protein and its antifungal activity, reported by Peng et al . [ 29 ], who produced mutant genes of a specific seed to obtain a change in the protein-surface hydrophobicity, and showed that a hydrophobic surface is essential to increase the antifungal property.…”
Section: Resultsmentioning
confidence: 99%
“…There is little information on the mechanism of action of these peptides beyond the fact that the P. americana knottin binds to the sphingolipids of fungal membranes and its antifungal activity is critically dependent on the presence of the hydrophobic patch (Peng et al 2005). As for biotechnological applications, one of the M. jalapa peptides increased resistance to the fungus Alternaria solani when introduced in tomato (Schaefer et al 2005).…”
Section: Knottins and Cyclotidesmentioning
confidence: 98%