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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 DESIGN AND SYNTHESIS OF AMPHIPATHIC A-HELICAL MODLE PEPTIDES TO OPTIMIZE CELL-PENETRATING PROPERTIES

등록일
2014년 8월 28일 16시 14분 22초
접수번호
1206
발표코드
BIO.P-642 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
진선미, 김서연, 유재훈*
서울대학교 화학교육과, Korea
Some a-helical amphipathic peptides with hydrophobic and cationic residues in hydrophilic face have unique properties such as antimicrobial activity and the cell penetrating ability. Especially, a model LK and KLA peptides have been known as widely used mitochondrial and microbial membrane targeting. We also observed KLA and LK peptides have some cell penetrating ability. Recent results of our laboratory demonstrated that formation of dimer α-helical bundles with these model peptides have unusually high cell penetrating abilities. Too optimize cell penetrating ability, we further changed various aspects of model peptides, such as sequences, length of amino acids, portion of cationic residues, sizes of hydrophobic residues at hydrophobic face. Results of experiments suggests that the length, the portion of cationic residues, the size of hydrophobic residues of the monomeric peptides affect significantly on the penetrating ability, while the orientation (parallel or anti-parallel) of dimers or consequences of peptide do not. More potent cell penetrating peptides could be designed and synthesized by applying these newly observed knowledge.

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