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제123회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Applicable factors for controlling the β-peptide 12/10-helix handedness

2019년 2월 12일 21시 55분 42초
ORGN.P-285 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 18일 (목요일) 11:00~12:30
Organic Chemistry
저자 및
Jieun Lee, Soo Hyuk Choi*
Department of Chemistry, Yonsei University, Korea
We present the controllable handedness of β-peptide 12/10-helix by adding methyl groups with specific stereochemistry to cis-2-aminocyclohexane carboxylic acid(cis-ACHC) residues and changing the position of double bond in center residue. Because the helix inversion occurs by ring flipping of the cyclohexane moieties, fixing the conformation of residues can make the oligomer more rigidified. In our laboratory, the first examples of atomic-resolution crystal data for the cis-ACHC oligomer with alternating chirality were discovered and in succession, we synthesized oligomers that have small differences in functional groups for comparing folding propensity. First, we synthesized two rigidified pentamers that consist of cis-2-amino-cis-4-methylcyclohexane carboxylic acid(cis,cis-mACHC) or cis-2-amino-trans-4-methylcyclohexane carboxylic acid(cis,trans-mACHC) with cyclohexene and compared them with a pentamer which has no methyl group. From the comparison, we proved that methyl groups affect directions of NH and C=O groups and therefore, they tend to make specific handedness of oligomers in solution. Secondly, we synthesized a pentamer which has a double bond at different position of central residue for probing the effect of double bond position to helical conformation. These controllable handedness of 12/10-helical β-peptide can be a valuable application to foldamer helices.