Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle
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Defensins, which are small cationic molecules produced byorganisms as part of their innate immune response, share acommon structural scaffold that is stabilized by three disulfidebridges. Coprisin is a 43-amino acid defensin-like peptide fromCopris tripartitus. Here, we report the intramolecular disulfideconnectivity of cysteine-rich coprisin, and show that it is thesame as in other insect defensins. The disulfide bond pairingsof coprisin were determined by combining the enzymaticcleavage and mass analysis. We found that the loss of anysingle disulfide bond in coprisin eliminated all antibacterial,but not antifungal, activity. Circular dichroism (CD) analysisshowed that two disulfide bonds, Cys20-Cys39 and Cys24-Cys41, stabilize coprisin’s α-helical region. Moreover, a BLASTsearch against UniProtKB database revealed that coprisin’sα-helical region is highly homologous to those of other insect defensins.
Abstract
Defensins, which are small cationic molecules produced byorganisms as part of their innate immune response, share acommon structural scaffold that is stabilized by three disulfidebridges. Coprisin is a 43-amino acid defensin-like peptide fromCopris tripartitus. Here, we report the intramolecular disulfideconnectivity of cysteine-rich coprisin, and show that it is thesame as in other insect defensins. The disulfide bond pairingsof coprisin were determined by combining the enzymaticcleavage and mass analysis. We found that the loss of anysingle disulfide bond in coprisin eliminated all antibacterial,but not antifungal, activity. Circular dichroism (CD) analysisshowed that two disulfide bonds, Cys20-Cys39 and Cys24-Cys41, stabilize coprisin’s α-helical region. Moreover, a BLASTsearch against UniProtKB database revealed that coprisin’sα-helical region is highly homologous to those of other insect defensins.
참고문헌 (20)
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