The Library
Design and synthesis of N-maleimido-functionalized hydrophilic polymers via copper-mediated living radical polymerization: A suitable alternative to PEGylation chemistry
Tools
UNSPECIFIED (2005) Design and synthesis of N-maleimido-functionalized hydrophilic polymers via copper-mediated living radical polymerization: A suitable alternative to PEGylation chemistry. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 127 (9). pp. 2966-2973. doi:10.1021/ja0430999 ISSN 0002-7863.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1021/ja0430999
Abstract
A series of a-functional maleimide polymethacrylates (M-n = 4.1-35.4 kDa, PDi = 1.06-1.27) have been prepared via copper-catalyzed living radical polymerization (LRP). Two independent synthetic protocols have been successfully developed and the polymers obtained in multigram scale, with an 80-100% content of maleimide reactive chain ends, depending on the method employed. A method for the synthesis of amino-terminated polymers, starting from Boc-protected amino initiators, has also been developed, as these derivatives are key intermediates in one of the two processes studied in the present work. The alternative synthetic pathway involves an initiator containing a maleimide unit "protected" as a Diels-Alder adduct. After the polymerization step, the maleimide functionality has been reintroduced by retro-Diels -Alder reaction, by simply refluxing those polymers in toluene for 7 h. These maleimido-terminated materials, poly(methoxyPEG((475))) methacrylates and poly(glycerol) methacrylates, differ for both the nature and size of the polymer side branches and showed an excellent solubility in water, a property that made them an ideal candidate for the synthesis of new polymer- (poly) peptide biomaterials. These functional polymers have been successfully employed in conjugation reactions in the presence of thiol-containing model substrates, namely, reduced glutathione (gamma-Glu-Cys-Gly) and the carrier protein, bovine serum albumin (BSA), in 100 mM phosphate buffer (pH 6.8-7.4) and ambient temperature.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | ||||
Publisher: | AMER CHEMICAL SOC | ||||
ISSN: | 0002-7863 | ||||
Official Date: | 9 March 2005 | ||||
Dates: |
|
||||
Volume: | 127 | ||||
Number: | 9 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 2966-2973 | ||||
DOI: | 10.1021/ja0430999 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |