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Alprazolam induced conformational change in hemoglobin
Satwata Maitra1, Biswarup Saha, Chitta Ranjan Santra
1Department of Life Science and Biotechnology, Jadavpur University, Kolkata 700032, West Bengal, India.
International Journal of Biological Macromolecules
|January 9, 2007
Summary
Alprazolam (ALP) binds strongly to hemoglobin (Hb), altering its structure and function. This interaction may increase oxygen release from red blood cells, raising concerns about the drug's safety.
Area of Science:
- Pharmacology
- Biochemistry
- Hematology
Background:
- Alprazolam (ALP) is a commonly prescribed benzodiazepine for sedation and depression.
- Its widespread use necessitates understanding potential interactions with vital biological molecules like hemoglobin (Hb).
Purpose of the Study:
- To investigate the interaction between Alprazolam and human hemoglobin.
- To elucidate the effects of Alprazolam binding on hemoglobin's structure and oxygen-carrying function.
Main Methods:
- Spectrophotometry and spectrofluorimetry were employed to study Alprazolam-hemoglobin binding.
- Circular dichroism spectroscopy assessed changes in hemoglobin's secondary structure.
- Dynamic light scattering measured alterations in hemoglobin particle size.
Main Results:
- Strong binding of Alprazolam to hemoglobin was confirmed.
- Significant alterations in the alpha-helical structure of hemoglobin subunits were observed.
- Alprazolam treatment led to increased blood oxygen partial pressure, indicating reduced oxygen affinity.
- Conformational changes resulted in an increased hemoglobin particle size.
Conclusions:
- Alprazolam interacts with hemoglobin, causing structural modifications.
- These changes impair hemoglobin's oxygen transport function.
- The findings highlight potential risks associated with the non-prescribed use of Alprazolam.
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