Relaxation Dynamics of Piroxicam Structures within Human Serum Albumin Protein

We report on steady-state and ps-time-resolved emission studies of piroxicam (1) drug within human serum albumin (HSA) protein in cyclodextrin and in neat solvents. The steady-state results indicate that 1 binds to HSA protein and that two binding sites are involved. The fluorescence decays correspo...

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Bibliographic Details
Published in:Journal of medicinal chemistry 2007-06, Vol.50 (12), p.2896-2902
Main Authors: El-Kemary, Maged, Gil, Michał, Douhal, Abderrazzak
Format: Article
Language:English
Subjects:
Analgesics
Anisotropy
Anti-Inflammatory Agents, Non-Steroidal - chemistry
beta-Cyclodextrins
Binding Sites
Biological and medical sciences
Bones, joints and connective tissue. Antiinflammatory agents
Energy Transfer
Humans
Hydrogen Bonding
Ions
Medical sciences
Models, Molecular
Molecular Conformation
Neuropharmacology
Pharmacology. Drug treatments
Piroxicam - chemistry
Protein Conformation
Serum Albumin - chemistry
Solutions
Tryptophan - chemistry
Water
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Summary:We report on steady-state and ps-time-resolved emission studies of piroxicam (1) drug within human serum albumin (HSA) protein in cyclodextrin and in neat solvents. The steady-state results indicate that 1 binds to HSA protein and that two binding sites are involved. The fluorescence decays corresponding to site I in subdomain IIA and to site II in subdomain IIIA have time constants of ∼60 ps and ∼360 ps, respectively. The results suggest that the anion forms bind to site I, whereas the zwitterionic ones bind to site II. The energy-transfer process from excited tryptophan to 1 can occur with moderate efficiency (50%). The rotational time of 1 encapsulated by HSA indicates diffusion within the protein. These findings can be used for a better understanding of piroxicam and HSA interactions.
ISSN:0022-2623
1520-4804
DOI:10.1021/jm061421f