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KMID : 0624620140470110625
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BMB Reports
2014 Volume.47 No. 11 p.625 ~ p.630
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Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle
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Lee Jae-Ho
Lee Da-Eun
Choi Hye-Min
Kim Ha-Hyung
Kim Ho
Hwang Jae-Sam
Lee Dong-Gun
Kim Jae-Il
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Abstract
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Defensins, which are small cationic molecules produced by organisms as part of their innate immune response, share a common structural scaffold that is stabilized by three disulfide bridges. Coprisin is a 43-amino acid defensin-like peptide from Copris tripartitus. Here, we report the intramolecular disulfide connectivity of cysteine-rich coprisin, and show that it is the same as in other insect defensins. The disulfide bond pairings of coprisin were determined by combining the enzymatic cleavage and mass analysis. We found that the loss of any single disulfide bond in coprisin eliminated all antibacterial, but not antifungal, activity. Circular dichroism (CD) analysis showed that two disulfide bonds, Cys20-Cys39 and Cys24- Cys41, stabilize coprisin’s α-helical region. Moreover, a BLAST search against UniProtKB database revealed that coprisin’s α-helical region is highly homologous to those of other insect defensins.
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KEYWORD
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Antimicrobial peptide, Circular dichroism, Coprisin, disulfide connectivity, Insect defensin
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