Published October 19, 2005
| Supplemental Material
Journal Article
Open
A General Route for Post-Translational Cyclization of mRNA Display Libraries
Chicago
An error occurred while generating the citation.
Abstract
Cyclic peptides are attractive scaffolds for the design of conformationally constrained molecular therapeutics. Previously, biological display libraries could only be cyclized via disulfide bonds, which are labile and can be reduced in an intracellular environment. In this paper, we construct high diversity, covalently cyclized mRNA display libraries (>10^(13) sequences) and analyze the cyclization reaction using MALDI-TOF MS and unnatural amino acid incorporation. Our route allows the extent of cyclization to be evaluated quantitatively and is broadly applicable to a variety of cyclization chemistries.
Additional Information
© 2005 American Chemical Society. Received July 1, 2005; Publication Date (Web): September 27, 2005. The authors would like to thank Niki Zacharias at Neurion Pharmaceuticals for the generous gift of pdCpA and α-hydroxy phenylalanine-dCA. This work was supported by NIH R01 GM60416, NIH Training Grant T32 GM08501, and the California Institute of Technology.Attached Files
Supplemental Material - ja054373hsi20050830_053129.pdf
Files
ja054373hsi20050830_053129.pdf
Files
(134.0 kB)
| Name | Size | Download all |
|---|---|---|
|
md5:10cb5e6549bb5c6d4361accbc90994eb
|
134.0 kB | Preview Download |
Additional details
- Eprint ID
- 75744
- Resolver ID
- CaltechAUTHORS:20170405-144317686
- NIH
- R01 GM60416
- NIH Predoctoral Fellowship
- T32 GM08501
- Caltech
- Created
-
2017-04-05Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field