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  • 09월 01일 18시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제118회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Amphiphilic Stereoisomers for Membrane Protein Study: Importance of Chirality in the Hydrophobic Backbone

등록일
2016년 9월 1일 10시 57분 13초
접수번호
2317
발표코드
ORGN.O-3 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 09시 : 30분
발표형식
구두발표
발표분야
유기화학 - Oral Presentations of Young Scholars in Organic Division
저자 및
공동저자
DASMANABENDRA, 채필석1,*
한양대학교 bionano engineering, India
1한양대학교 생명나노공학과, Korea

Membrane proteins (MPs) are crucial cellular components, responsible for a range of key biological functions including inter- or intra-cellular material transfer and signal transduction and represent more than one-half of human drug targets. The high-resolution structures are essential to understand the underlying molecular mechanisms of these biomolecules and rational drug design efforts. Detergents are required to extract membrane proteins from the membranes and to maintain them in their native states in non-native environments. As conventional detergents have limited ability to stabilize membrane proteins, novel agents with enhanced efficacy need to be developed. Here we made efforts to develop stereoisomeric amphiphiles for membrane protein study and explore stereo-chemical outcome on stabilization of four different membrane proteins targeted here. Our collective efforts involving synthetic chemists, structural biologists and membrane protein scientists not only provide novel detergent tools useful for membrane protein study, but also include new detergent design guidelines for future development.

References:
1. M. Das, Y. Du, J. S. Mortensen, O. Ribeiro, P. Hariharan, C. J. Loland, L. Guan, B. Byrne, B. K. Kobilka, P. S. Chae, Amphiphilic Stereoisomers for Membrane Protein Study: Importance of Chirality in the Hydrophobic Region. Chem. Sci., under review process.
2. M. Ehsan, Y. Du, N. J. Scull, E. Tikhonova, J. Tarrasch, J. S. Mortensen, C. J. Loland, G. Skiniotis, L. Guan, B. Byrne, B. K. Kobilka, P. S. Chae, Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies. J. Am. Chem. Soc. 2016, 138, 3789-3796.


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