Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
Angew Chem Int Ed Engl. 2017 Feb 13;56(8):2087-2091. doi: 10.1002/anie.201610154. Epub 2017 Jan 12.
Peptide foldamers containing both cis-β-aminocyclopentanecarboxylic acid and α-amino acid residues combined in various sequence patterns (ααβ, αααβ, αβααβ, and ααβαααβ) were screened using CD and NMR spectroscopy for the tendency to form helices. ααβ-Peptides were found to fold into an unprecedented and well-defined 16/17/15/18/14/17-helix. By extending the length of the sequence or shifting a fragment of the sequence from one terminus to another in ααβ-peptides, the balance between left-handed and right-handed helix populations present in the solution can be controlled. Engineering of the peptide sequence could lead to compounds with either a strong propensity for the selected helix sense or a mixture of helical conformations of opposite senses.
含有顺式-β-氨基环戊烷羧酸和α-氨基酸残基的肽折叠体，以各种序列模式（ααβ、αααβ、αβααβ 和 ααβαααβ）组合，通过 CD 和 NMR 光谱筛选其形成螺旋的趋势。ααβ-肽被发现折叠成一种前所未有的、明确的 16/17/15/18/14/17-螺旋。通过延长序列的长度或在 ααβ-肽中将序列的片段从一个末端转移到另一个末端，可以控制溶液中存在的左手和右手螺旋体的平衡。通过对肽序列的工程设计，可以得到对所选螺旋方向具有强烈倾向的化合物，或者得到相反方向的混合螺旋构象的化合物。
