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학술발표회초록보기

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  • 03월 02일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Sergeant and soldiers effects: Helix-inducing placement of chiral residues in peptoid sequences

등록일
2012년 3월 2일 14시 49분 30초
접수번호
1568
발표코드
MAT.P-1218 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 25일 (수요일) 18:00~21:00
발표형식
포스터
발표분야
재료화학
저자 및
공동저자
신혜민, 서지원1, 윤명한
광주과학기술원 신소재공학부, Korea
1광주과학기술원 기초교육학부, Korea
Natural molecules such as proteins, nucleic acids and carbohydrates have specific functions, which are mainly originated from their 3D structures. Hence, many biomimetic molecules such as artificial peptides and peptoids are being investigated to fold into specific secondary structures. Peptoids, oligo-N-substitute glycines, have achirality of backbone and lack of hydrogen bond donors, so difficult to form α-helical structure. Yet, peptoids with α-chiral, aromatic side-chains form stable polyproline-like helices in both organic and aqueous solutions. Even though peptoid structures such as α-helix, threaded-loop, and cyclic peptoid have been discovered, there is still lack of understanding on the precise control of peptoid structures that lie in between fully helical and unstructured. In this study, we report the synthesis and characterization of a family of structured peptoids with varying an α-chiral residue location to investigate how effectively peptoid helicity is controlled via regiochemistry of α-chiral residue. Circular dichroism studies of the sequenced peptoid heptamers reveal that stronger helicities are induced by α-chiral residue on the first position from the C-terminus than the other positions and those peptoids’ helicities are maintained stably in acetonitrile solution at temperatures up to 75℃. These results will be the foundation of peptoids’ sequence-structure relationships.

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