Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes.

@article{AbouZied2008CharacterizationOS,
  title={Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes.},
  author={Osama K Abou-Zied and Othman I K Al-Shihi},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 32},
  pages={10793-801}
}
Subdomain IIA binding site of human serum albumin (HSA) was characterized by examining the change in HSA fluorescence in the native, unfolded, and refolded states. The study was carried out in the absence and presence of small molecular probes using steady-state and time-resolved fluorescence measurements. 2-Pyridone, 3-pyridone, and 4-pyridone bear similar molecular structures to those found in many drugs and are used here as probes. They are found to specifically bind in subdomain IIA and… CONTINUE READING
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