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제123회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Changing folding structure of 12/10-Helical β-Peptides by residue tansformation

등록일
2019년 2월 12일 21시 55분 42초
접수번호
4010
발표코드
ORGN.P-286 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 18일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
Organic Chemistry
저자 및
공동저자
Yonghan Kim, Soo Hyuk Choi*
Department of Chemistry, Yonsei University, Korea
Foldamer refers to a compound capable of forming a certain structure such as a protein found in nature. In the case of oligomers containing β-amino acid, a new form of hydrogen bonding structure that shows a different tendency from alpha was observed. Oligomers containing ACHpC(2-aminocycloheptanecarboxylic acid) has low energy barrier required for interconversion between M- and P-helix. In order to take advantage of these properties, we are trying to find an oligomer composed of ACHpC which forms a stable skeleton. The 12/10-helical pentamers that consist of cis-ACHpC were identified using IR, CD and NMR study. Previous research has shown that the mACHC(2-amino-4-methylcyclohexanecarboxylic acid) can control the N-H binding arrangement to axial or equatorial using the 1,3-diaxial interaction of methyl. This allowed the ring structure and handedness to make up the oligomer were fixed in one direction. We predicted that when introducing the control part in the middle of the pentamers instead of the N-terminus, it is easier to control the helix. Because of β3- and β2-alanine are expected to be able to control helix by forming gauche- conformation in helical structures, we synthesized pentamers containing β3- or β2-alanine in the middle of the pentamers. We then analyzed the changes in structure and hydrobonding by IR, CD and NMR study.

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