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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제27권 제4호
- 발행연도
- 2017.1
- 수록면
- 759 - 767 (9page)
이용수
초록· 키워드
오류제보하기
Lactophoricin (LPcin), which is a part of proteose peptone isolated from bovine milk, is a cationic amphipathic α-helical antimicrobial peptide. Its truncated variants and mutated analogs were designed and their antimicrobial activities were evaluated by using various assays, like broth dilution methods and disk diffusion methods as well as hemolysis assay. Three analogs, LPcin-C8 (LPcin-YK1), LPcin-T2&6W (LPcin-YK2), and LPcin-T2&6W-C8 (LPcin-YK3), which showed better antibiotic activities than LPcin, were selected. Their secondary structures were also characterized by using CD spectropolarimetry. These three analogs of LPcin could be used as an alternative source of powerful antibacterial agents.
목차
등록된 정보가 없습니다.
참고문헌 (27)
참고문헌 신청
Aley SB / 1994 / Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides / Infect. Immun 62 : 5397 ~ 5403
Andreu D / 1998 / Animal antimicrobial peptides: an overview / Biopolymers 47 : 415 ~ 433
Bechinger B. / 1997 / Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin / J. Membr. Biol 156 : 197 ~ 211
Brad P / / Washington Post
Brown KL / 2006 / Cationic host defense (antimicrobial) peptides / Curr. Opin. Immunol 18 : 24 ~ 30
Andreu D / 1998 / Animal antimicrobial peptides: an overview / Biopolymers 47 : 415 ~ 433
Bechinger B. / 1997 / Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin / J. Membr. Biol 156 : 197 ~ 211
Brad P / / Washington Post
Brown KL / 2006 / Cationic host defense (antimicrobial) peptides / Curr. Opin. Immunol 18 : 24 ~ 30
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