Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles
| Autor: | Yoshio Komine, Toru Maruyama, Masaki Otagiri, Koji Nishi, H. Brian Halsall, Norifumi Sakai |
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| Rok vydání: | 2002 |
| Předmět: |
Dicumarol
Chlorpromazine Protein Conformation medicine.medical_treatment Biophysics Biochemistry Micelle Protein Structure Secondary Analytical Chemistry Native state medicine Molecular Biology Micelles Progesterone chemistry.chemical_classification Transition (genetics) Circular Dichroism Biological membrane Orosomucoid Molten globule Kinetics Steroid hormone chemistry Ionic strength Glycoprotein Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1601:185-191 |
| ISSN: | 1570-9639 |
| DOI: | 10.1016/s1570-9639(02)00465-x |
| Popis: | Alpha(1)-acid glycoprotein (AGP) is a glycoprotein that consists of 183 amino acid residues and five carbohydrate chains and binds to neutral and basic drugs. We examined the structural properties and ligand-binding capacity of AGP in interactions with reverse micelles. Also, detailed information was obtained by comparing several different states of AGP. Interaction with reverse micelles induced a unique conformational transition (beta-sheet to alpha-helices) in AGP and decreased the binding capacity for the basic drug, chlorpromazine and the steroid hormone, progesterone to AGP. These structural conformations are very similar to those observed under conditions of acidity and high ionic strength (pH 2.0, 1.5 M NaCl). This structure seems to be an intermediate between the native state and the denatured state, possibly a molten globule. The present results suggest that when AGP interacts with the biomembrane, it undergoes a structural transition to a unique structure that differs from the native and denatured states and has a reduced ligand-binding capacity. |
| Databáze: | OpenAIRE |
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