Published January 5, 2009
| Accepted Version + Supplemental Material
Journal Article
Open
Biosynthesis and Stability of Coiled-Coil Peptides Containing (2S,4R)-5,5,5-Trifluoroleucine and (2S,4S)-5,5,5-Trifluoroleucine
Abstract
We report the effects of 5,5,5-trifluoroleucine (TFL) stereochemistry on coiled-coil peptide biosynthesis and stability. We demonstrate that two diastereoisomers of TFL are activated and incorporated into peptides expressed in E. coli. Coiled-coil homodimers of these peptides exhibited increased stability. An equimolar mixture of the two fluorinated peptides formed a heterodimer of modestly enhanced thermal stability relative to the homodimers.
Additional Information
© 2009 Wiley. This work was supported by the NIH grants GM62523 and 5FM GM67375-2 (D.A.T. and J.K.M.), and GM65500 (K.K.), NSF graduate fellowship (S.S.), GAANN fellowship (G.A.C.), and a NSF CAREER award (K.K.).Attached Files
Accepted Version - nihms327142.pdf
Supplemental Material - sm001.pdf
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Additional details
- PMCID
- PMC3212351
- Eprint ID
- 15954
- Resolver ID
- CaltechAUTHORS:20090918-093938869
- GM62523
- NIH
- 5FM GM67375-2
- NIH
- GM65500
- NIH
- NSF Graduate Research Fellowship
- Department of Education
- Created
-
2009-09-18Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field