| Autor: |
Benesch RE; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032., Kwong S, Hudson BB, Krumdieck CL |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 1988 Jan 05; Vol. 263 (1), pp. 69-71. |
| Abstrakt: |
We have synthesized and tested a new series of compounds that inhibit the polymerization of deoxyhemoglobin S by noncovalent interaction. They consist of three structural elements: A p-aminobenzoyl residue to anchor the compound in the central cavity between the beta chains, a number of glutamates in gamma linkage to provide tight binding, and one or two hydrophobic amino acid residues which block the intermolecular hydrophobic interaction of valine beta 6. The most active compound was p-aminobenzoyl-(gamma-Glu)5-Phe-Phe. It increases the solubility of deoxy-HbS by a factor of 1.3 at a concentration of only 5-6 mM and is effective even in the presence of physiological concentrations of 2,3-diphosphoglycerate. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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