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- W3119203122 endingPage "1190" @default.
- W3119203122 startingPage "1184" @default.
- W3119203122 abstract "Abstract Peptides that are composed of backbone‐extended amino acids can adopt conformations resembling natural α‐peptidic motifs, making them promising scaffolds for biological and medicinal chemistry. In order to unlock the full potential of this class of molecules, the ability to control their secondary structures is essential. Here we show that stereoselective fluorination can be harnessed as a tool for influencing the helical character of a γ‐hexapeptide. Fluorination is shown to either stabilize or disrupt the 9‐helical conformation depending on the C−F stereochemistry, and fluorination also sets the handedness of the helix. These results provide fundamental knowledge that could expedite the future development of backbone‐extended peptides for medicinal applications." @default.
- W3119203122 created "2021-01-18" @default.
- W3119203122 creator A5026793181 @default.
- W3119203122 creator A5072678331 @default.
- W3119203122 date "2021-01-25" @default.
- W3119203122 modified "2023-09-29" @default.
- W3119203122 title "Controlling γ‐Peptide Helicity with Stereoselective Fluorination" @default.
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- W3119203122 doi "https://doi.org/10.1002/ejoc.202001619" @default.
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