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Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle.


ABSTRACT: 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 ?-helical region. Moreover, a BLAST search against UniProtKB database revealed that coprisin's ?-helical region is highly homologous to those of other insect defensins.

SUBMITTER: Lee J 

PROVIDER: S-EPMC4281341 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle.

Lee Jaeho J   Lee Daeun D   Choi Hyemin H   Kim Ha Hyung HH   Kim Ho H   Hwang Jae Sam JS   Lee Dong Gun DG   Kim Jae Il JI  

BMB reports 20141101 11


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 cleavag  ...[more]

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