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  • 03월 02일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structure-Activity relationships of coprisin isolated from the dung beetle, Copris tripartitus

2012년 2월 17일 17시 45분 01초
BIO.P-695 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 25일 (수요일) 18:00~21:00
저자 및
이은정, 김진경, 이주호, 정기웅, 김양미
건국대학교 생명공학과, Korea
The novel 43-residue defensin-like peptide, coprisin isolated recently from the Dung Beetle, Copris tripartitus exhibits antimicrobial activities against standard bacterial strains as well as drug-resistant bacterial strains. To study structure-activity relationships, we determined the three-dimensional structure of coprisin in aqueous solution by NMR spectroscopy, showing that coprisin has an amphipathic alpha-helical structure from Ala19 to Arg28 and beta-sheet from Gly31 to Gln35 and Val38 to Arg42. Coprisin has a highly electropositive regions positioned at the end of the helix (Arg28), turns between the helix and the first strand of the sheet (Lys29, Lys30), and C-terminus (Arg42). We studied anti-inflammatory activity of coprisin, examining the effect of coprisin on lipopolysaccharide (LPS)-induced inflammatory response by measuring nitric oxide (NO) release and inflammatory cytokines. As coprisin was treated in LPS-stimulated mouse macrophage cells, the process of gene transcriptions for inflammatory cytokines was inhibited. We have demonstrated that coprisin shows profound antibacterial activities since coprisin has an amphipathic helix and electropositive surface which may play important role in its structure stability and effective interaction with bacterial lipid membrane. Furthermore, coprisin is a potent anti-inflammatory peptide with antibacterial activities, and this work may help to understand its mechanism of action in near future.