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학술발표회초록보기

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

제113회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Relationship between Structure and function of hybrid antimicrobial peptide, Papiliocin(Pap)-Magainin(MA)-P2 and its analogs

등록일
2014년 2월 20일 16시 29분 04초
접수번호
1405
발표코드
BIO.P-579 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 16일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
신아름, 이은정, 김양미*
건국대학교 생명공학과, Korea
Papiliocin is consisted of 37-amino acids antimicrobial peptide which is purified from the swallowtail butterfly, Papilio xuthus. Magainin 2 is consisted of 23-amino acids antimicrobial peptide which is isolated from African clawed frog. PapMA is a 20-residue hybrid peptide incorporating residues 1-8 of papiliocin and residues 1-12 of magainin 2. PapMA have potent antimicrobial activity without toxicity against mammalian cells. PapMA-P2, in which the Gly-Ile-Gly sequence of PapMA is substituted with Pro, was designed. According to the results of cytoxicity against bacteria and mammalian cells, and phospholipid membrane permeability, PapMA-P2 with high antimicrobial acitivities targets the bacterial cell membrane. To discover peptide antibiotics having lower toxicity and higher selectivity, we substituted ala, lys and leu peptoids for Pro. Peptoid analogues also showed that high antimicrobial activities and low toxicities against mammalian cells. CD spectra and NMR spectroscopy suggested that PapMA-P2 and its analogues have α-helical conformations in membrane-mimicking environment. PapMA-P2-lys peptoid exists in dynamic equilibrium of cis and trans conformers with a ratio of 1:3. Structure-activity relationships of these peptides will give insights to understand its mechanism of actions and help to develop more potent peptide antibiotics as useful therapeutic agents.

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