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  • 02월 20일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제113회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Function of three phenylalanines and Val10 in piscidin-1 on its mechanisms of antibacterial activities and cytotoxicities

2014년 2월 20일 16시 23분 15초
BIO.P-578 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 16일 (수요일) 16:00~19:00
저자 및
이은정, 신아름, 김양미*
건국대학교 생명공학과, Korea
Piscidin-1 (Pis-1) is an antibacterial peptide derived from mast cells of hybrid striped bass that comprises 22 amino acids with phenylalanine-rich amino-terminal. To verify the key residues for the antibacterial activity and those for the cytotoxicity of piscidin, we investigate the role of each Phe residue as well as the Val10 which is located at the hydrophilic phase. Tryptophan fluorescence blue shift was monitored for the peptides with Trp substitution of Phe1, Phe2, and Phe6, respectively. Each Phe was substituted with Ala or Lys to investigate their functional roles. As results, and Phe2 plays key roles in cytotoxicity of Pis-1 while Phe2 and Phe6 plays key roles in antibacterial activities of Pis-1. We also designed piscidin analogue, Pis-V10K with Lys substitution of Val10 which results in an elevated amphipathic α-helical structure showed similar antibacterial activity when compared with Pis-1; however, it showed much lower cytotoxicity than Pis-1. NMR spectroscopy revealed that Pis-V10K in a 300 mM SDS micelle had a linear amphipathic alpha-helical structure from Phe2 to Thr21. In this study, we have demonstrated that piscidin analogs which substituted with Lys in Pis-F1K/V10K and Pis-F2K/V10K are potent peptide antibiotics with both anti-inflammatory and antimicrobial activities and we provide mechanism of action of piscidin analogs.