787632-53-5Relevant academic research and scientific papers
A highly stable short α-helix constrained by a main-chain hydrogen-bond surrogate
Chapman, Ross N.,Dimartino, Gianluca,Arora, Paramjit S.
, p. 12252 - 12253 (2004)
Herein we describe a strategy for the preparation of artificial α-helices involving replacement of one of the main-chain hydrogen bonds with a covalent linkage. To mimic the C=O...H-N hydrogen bond as closely as possible, we envisioned a covalent bond of the type C=X-Y-N, where X and Y are two carbon atoms connected through an olefin metathesis reaction. Our results demonstrate that the replacement of a hydrogen bond between the i and i + 4 residues at the N-terminus of a short peptide with a carbon-carbon bond results in a highly stable constrained α-helix at physiological conditions as indicated by CD and NMR spectroscopies. The advantage of this strategy is that it allows access to short α-helices with strict preservation of molecular recognition surfaces required for biomolecular interactions. Copyright
Rational design of an orthosteric regulator of hIAPP aggregation
Zhao, De-Sheng,Chen, Yong-Xiang,Li, Yan-Mei
, p. 2095 - 2098 (2015/02/05)
Developing compounds regulating amyloid toxic oligomer but not fibril formation should constitute an effective strategy for the treatment of diabetes. Based on the full understanding of the folding mechanism, we designed an orthosteric helix regulator that can promote hIAPP to assemble into large non-cytotoxic oligomers. As a result, the islet cells were protected. This journal is
Methods for preparing internally constrained peptides and peptidomimetics
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Page/Page column 30, (2016/01/20)
The present invention relates to a method for preparing a peptide having a stable, internally constrained alpha-helical, beta-sheet/beta-turn, 310-helical, or pi-helical region and a method of stabilizing an alpha-helical, beta-sheet/beta-turn,
