Published October 1997
| Version public
Journal Article
Biosynthetic Incorporation and Chemical Modification of Alkene Functionality in Genetically Engineered Polymers
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1.
University of Massachusetts Amherst
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2.
University of California, Santa Barbara
Abstract
Repetitive polypeptides of sequence [(AlaGly)_3ProGluGly]_(16) 3a, have been prepared in Escherichia coli as overexpressed recombinant proteins. Replacement of more than 90% of the naturally occurring proline (Pro) residues with 3,4-dehydroproline (Dhp) in sequence 3a was achieved by in vivo expression of the target protein in medium containing Dhp and lacking Pro. The resulting material (3b) was treated with H_2O_2 or Br_2 to yield polymers containing 3,4-dihydroxyproline (Dhy, 3c) and 3,4-dibromoproline (Dbr, 3d), respectively, in place of the Dhp residue. These results represent the first demonstration of the incorporation and modification of alkene functionality in recombinant proteins.
Additional Information
© 1997 Marcel Dekker. This work was supported by Contract No. DAAH04-93-G-0217 from the U. S. Army Research Office and by a grant (DMR-8914359) from the Polymers and Genetics Programs of the National Science Foundation. T. J. D. acknowledges the National Institutes of Health for a National Research Service Award postdoctoral training fellowship. NMR spectra were recorded in the University of Massachusetts NMR Facility, which is supported in part by the NSF Materials Research Science and Engineering Center at the University.Additional details
Identifiers
- Eprint ID
- 53440
- DOI
- 10.1080/10601329708010331
- Resolver ID
- CaltechAUTHORS:DEMjmsa1997
Related works
- Describes
- 10.1080/10601329708010331 (DOI)
Funding
- Army Research Office (ARO)
- DAAH04-93-G-0217
- NSF
- DMR-8914359
- NIH Postdoctoral Fellowship
Dates
- Created
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2015-01-31Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field