Structure-antifungal activity relationships of cecropin A hybrid peptides against Trichoderma sp.

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Structure-antifungal activity relationships of cecropin A hybrid peptides against Trichoderma sp.
Song Yub Shin; Dong Gun Lee; Sung Gu Lee; Kil Lyong Kim; Myung Kyu Lee; Kyung Soo Hahm
Bibliographic Citation
Journal of Microbiology, vol. 35, no. 1, pp. 21-24
Publication Year
The hybrid peptides, CA-ME, CA-MA and CA-BO, with the N-terminal sequence 1-8 of cecropin A and the N-terminal sequences 1-12 of melittin, magainin 2 and bombinin, respectively, have more improved antibacterial activities. CA-MA was found to have stronger antifungal activity against Trichoderma sp than other hybrid peptides and their parental peptides. In order to elucidate the relationships between the peptide structure and antifungal activity, several analogues of CA-MA or CA-BO were also designed and synthesized by the solid phase method. Antifungal activity was measured against T. reesei and T. viride, and hemolytic activity was measured by a solution method against human red blood cells. The residue 16 of CA-MA, Ser, was found to be important for antifungal activity. When the residue was substituted with Leu, antifungal activity was dramatically decreased. CA-MA, P1, P4 and P5 designed in this study showed powerful antifungal activity against T. reesei and T. viride with low hemolytic activity against human red blood cells. These hybrid peptides will be potentially useful model to further design peptides with powerful antifungal activity for the effective therapy of fungal infection and understand the mechanisms of antifungal actions of hybrid peptides.
Antifungal activityCecropin A hybrid peptideHemolytic activityTrichoderma sp.
Microbiological Society Korea
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