|
|
ABSTRACT
| Title |
: |
Concise Review on Fluorescence Spectroscopy – A Commonly Utilized Technique in Study of Drugs-Protein Interaction |
| Authors |
: |
Bhutkar Shraddha P., Dhande Swati R., Kadam Vilasrao J. |
| Keywords |
: |
Human Serum Albumin, Sudlow’s sites, Fluorescence Spectroscopy, Diflunisal, Captopril, Tenofovir. |
| Issue Date |
: |
May 2015 |
| Abstract |
: |
Human Serum Albumin (HSA) is the most abundant plasma protein with molecular weight 67kDa. X-ray crystallography studies infer that it is constituted of three homologous domains namely I, II, III. These domains are further subdivided into subdomains A and B respectively. Subdomain IIA represents Sudlow’s site I that is Warfarin binding site and Subdomain IIIA represents Sudlow’s site II that is Ibuprofen binding site. Serum albumin exhibits excellent binding properties and hence it has main physiological function of transport of drug molecules to the tissues. Upon absorption of drugs into the systemic circulation, they bind to serum albumin and exist in HSA-drug complex form. This review focuses upon the application of Fluorescence Quenching Techniques by enlightening the binding studies of Diflunisal, Captopril and Tenofovir to the Human Serum Albumin. Fluorescence spectroscopic techniques are preferred because of the ease of use, greater sensitivity and rapidness. |
| Page(s) |
: |
927-933 |
| ISSN |
: |
0975-9492 |
| Source |
: |
Vol. 6, No.5 |
|
Copyright to ENGG Journals Publications
