期刊
BIOORGANIC CHEMISTRY
卷 119, 期 -, 页码 -出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2021.105491
关键词
Polyproline; Fluorous; Circular dichroism; Conformation analysis; Peptides
资金
- Ministry of Science and Technology, Taiwan [MOST 110-2113-M-007-009]
This article investigates how the interaction between fluorine atoms alters protein structures and develops approaches to synthesize fluorinated peptides. The study systematically explores the effects of the number, location, and types of fluorine groups on the conformation of polyproline peptides.
The unique interaction between fluorine atoms has been exploited to alter protein structures and to develop synthetic and analytical applications. To expand such fluorous interaction for novel applications, polyproline peptides represent an excellent molecular nanoscaffold for controlling the presentation of perfluoroalkyl groups on their unique secondary structure. We develop approaches to synthesis fluorinated peptides to systematically investigate how the number, location and types of the fluorous groups on polyproline affect the conformation by monitoring the transition between the two major polyproline structures PPI and PPII. This work provides valuable information on how fluorous interaction affects the peptide structure and also benefits the design of functional fluorous molecules.
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