Journal article
Different protein-binding selectivities for N-acyl heparin derivatives having N-phenylacetyl and heterocycle analogs of N-phenylacetyl substituted in place of N-sulfo groups
Bioorganic & medicinal chemistry letters, Vol.17(2), pp.419-423
2007
DOI: 10.1016/j.bmcl.2006.10.026
PMID: 17070049
Abstract
Replacing
N-sulfo groups in heparin with
N-arylacyl moieties has been shown to afford charge-reduced heparin derivatives that maintain affinity for select heparin-binding proteins. In this study 50% and 100% N-desulfonated heparins were selectively N-acylated with phenylacetic acid and four phenylacetic acid analogs where the phenyl ring was replaced by a heterocycle. Protein-binding studies reveal that structural differences in the ring systems of the
N-acyl groups appended to heparin afford significant affects on affinity and selectivity for different heparin-binding proteins.
Details
- Title: Subtitle
- Different protein-binding selectivities for N-acyl heparin derivatives having N-phenylacetyl and heterocycle analogs of N-phenylacetyl substituted in place of N-sulfo groups
- Creators
- Liusheng Huang - University of IowaCristina Fernández - University of IowaRobert J. Kerns
- Resource Type
- Journal article
- Publication Details
- Bioorganic & medicinal chemistry letters, Vol.17(2), pp.419-423
- Publisher
- Elsevier Ltd
- DOI
- 10.1016/j.bmcl.2006.10.026
- PMID
- 17070049
- ISSN
- 0960-894X
- eISSN
- 1464-3405
- Language
- English
- Date published
- 2007
- Academic Unit
- Pharmaceutical Sciences and Experimental Therapeutics; Medicinal and Natural Products Chemistry
- Record Identifier
- 9984365882802771
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