Synthesis of New Polymer-Bound Adenine Nucleotides Using Starburst PAMAM Dendrimers
| Autor: | Hiroyasu Ogino, Masahiro Yasuda, Wael Abdelmoez, Haruo Ishikawa, Kosaku Ishimi |
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| Rok vydání: | 2002 |
| Předmět: |
Dendrimers
Time Factors Polymers Stereochemistry Cofactor Substrate Specificity chemistry.chemical_compound Adenosine Triphosphate Drug Stability Adenine nucleotide Dendrimer Polyamines Organic chemistry Nucleotide Carbodiimide chemistry.chemical_classification Hexokinase Acetate kinase biology Spectrum Analysis Phosphotransferases Temperature Hydrogen-Ion Concentration Adenosine Diphosphate Kinetics End-group chemistry Chromatography Gel biology.protein Biotechnology |
| Zdroj: | Biotechnology Progress. 18:706-712 |
| ISSN: | 8756-7938 |
| DOI: | 10.1021/bp020062o |
| Popis: | Two types of new polymer-bound adenine nucleotides were synthesized by coupling adenine nucleotides (ATP and ADP) with starburst polyamidoamine (PAMAM) dendrimers. The first type was obtained by coupling native adenine nucleotides directly with a carboxy-terminated PAMAM dendrimer. In the second type, the nucleotides were modified by introducing a spacer arm containing a carboxylic end group (N(6)-R-ATP and N(6)-R-ADP) and coupled with an amine-terminated PAMAM dendrimer. Both types of the dendrimers were coupled with native or the modified nucleotides using the well-known carbodiimide activation technique. The optimum coupling pH and temperature were 4 and 30 degrees C, respectively, for preparing the carboxy-terminated PAMAM-bound ATP or ADP, and were 9 and 50 degrees C, respectively, for preparing the amine-terminated PAMAM-bound N(6)-R-ATP or N(6)-R-ADP. The ATP or ADP contents in the synthesized polymers were found to be 4 mol of ATP or of ADP/mol of carboxy-terminated PAMAM-bound ATP or ADP and 25 mol of ATP or of ADP/mol of amine-terminated PAMAM-bound N(6)-R-ATP or N(6)-R-ADP. The coenzymatic activities relative to the native ATP of the carboxy-terminated PAMAM-bound ATP against glucokinase and hexokinase were 16 and 7%, respectively, and those of the amine-terminated PAMAM-bound N(6)-R-ATP 2 and 1%, respectively. The coenzymatic activities relative to the native ADP of the carboxy-terminated PAMAM-bound ADP and the amine-terminated PAMAM-bound N(6)-R-ADP against acetate kinase were 24 and 3.5%, respectively. |
| Databáze: | OpenAIRE |
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