Interaction between a potent corticosteroid drug – Dexamethasone with bovine serum albumin and human serum albumin: A fluorescence quenching and fourier transformation infrared spectroscopy study

Naik, Praveen N.; Chimatadar, Shivamurti A.; Nandibewoor, Sharanappa T.

doi:10.1016/j.jphotobiol.2010.05.014

Cited by 210 publications

(86 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was observed that the absorption intensities of BSA/HSA increased upon the addition of ergosterol. The results suggested that it was due to the complex formation between ergosterol and BSA/HSA [32]. So, the binding interactions of ergosterol to BSA/HSA might lead to the changes in the conformation of BSA/HSA.…”

Section: Uv-vis Absorption Spectroscopymentioning

confidence: 97%

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng

2012

Mol Biol Rep

View full text Add to dashboard Cite

This study was designed to examine the interactions of ergosterol with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with the drug concentrations in the range of 2.99-105.88 μM and the concentration of proteins was fixed at 5.0 μM. The analysis of emission spectra quenching at different temperatures revealed that the quenching mechanism of HSA/BSA by ergosterol was the static quenching. The number of binding sites n and the binding constants K were obtained at various temperatures. The distance r between ergosterol and HSA/BSA was evaluated according to Föster non-radioactive energy transfer theory. The results of synchronous fluorescence, 3D fluorescence, FT-IR, CD and UV-Vis absorption spectra showed that the conformations of HSA/BSA altered in the presence of ergosterol. The thermodynamic parameters, free energy change (ΔG), enthalpy change (ΔH) and entropy change (ΔS) for BSA-ergosterol and HSA-ergosterol systems were calculated by the van't Hoff equation and discussed. Besides, with the aid of three site markers (for example, phenylbutazone, ibuprofen and digitoxin), we have reported that ergosterol primarily binds to the tryptophan residues of BSA/HSA within site I (subdomain II A).

show abstract

Section: Uv-vis Absorption Spectroscopymentioning

confidence: 97%

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng

2012

Mol Biol Rep

View full text Add to dashboard Cite

show abstract

“…In addition, it is known that the bioactivity of most drugs used to treat some diseases can be realized by the study of interaction between drugs and protein, and there was a great interest in the application of spectroscopic techniques and molecular docking methods in the study of interaction between drugs and human serum albumin (HSA). [10][11][12][13][14] Obviously, surface-enhanced Raman scattering (SERS) technique is also an important method of studying the interaction of 6-PTU with HSA because HSA transports the 6-PTU to the target organism. It can help us find out the mechanism of the interaction between drugs and blood plasma or serum albumin.…”

Section: Introductionmentioning

confidence: 99%

Characterization of 6‐propylthiouracil and its interaction with human serum albumin on Au surface by surface‐enhanced Raman scattering

2015

J Raman Spectroscopy

View full text Add to dashboard Cite

In this study, surface-enhanced Raman scattering (SERS) spectra of 6-propylthiouracil (6-PTU) on Au surface and the interaction between 6-PTU and human serum albumin (HSA) were studied. The Raman bands were assigned by the density functional theory calculations at the B3LYP/6-311++g(d,p) level. Furthermore, the effects of concentration on the SERS spectra of 6-PTU were analyzed. It shows that with the changes of the concentrations of 6-PTU, the SERS spectra of 6-PTU present significant changes, and it can be concluded that with the changing of concentrations, the orientation of 6-PTU on Au surface also changes. In addition, the SERS spectra of the interaction between 6-PTU and HSA show that the binding sites of 6-PTU to HSA are the functional groups N3H and C¼O. The information will not only be references to the study of the mechanism of the interaction between drugs and blood plasma or serum albumin but also a guidance to understand the metabolism of drugs in human body.

show abstract

“…These changes to HSA absorbance spectra indicate an interaction between the protein and ZM5. Fluorescence of HSA is almost entirely due tryptophan but also due tyrosine and phenylalanine residues [37]. Drugs have their binding site in subdomains IIA and IIIA of HSA [38], where the former is a hydrophobic cavity where the sole tryptophan (Trp-214) of HSA is found and accounts for the natural Figure S5 and Table SIII fluorescence of the protein [37,38].…”

Section: Study Of the Interaction Of Zm5 With Human Serum Albumin (Hsa)mentioning

confidence: 99%

“…Fluorescence of HSA is almost entirely due tryptophan but also due tyrosine and phenylalanine residues [37]. Drugs have their binding site in subdomains IIA and IIIA of HSA [38], where the former is a hydrophobic cavity where the sole tryptophan (Trp-214) of HSA is found and accounts for the natural Figure S5 and Table SIII fluorescence of the protein [37,38]. This residue is very sensitive to local environment changes and so variations in fluorescence spectra are associated to conformational transitions or interaction between drugs and HSA [37,39].…”

Section: Study Of the Interaction Of Zm5 With Human Serum Albumin (Hsa)mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of antiproliferative potential and biological targets of a copper compound containing 4′-phenyl terpyridine

et al. 2015

View full text Add to dashboard Cite

Several copper complexes have been assessed as anti-tumor agents against cancer cells. In this work, a copper compound [Cu(H2O){OS(CH3)2}L](NO3)2 incorporating the ligand 4'-phenyl-terpyridine antiproliferative activity against human colorectal, hepatocellular carcinomas and breast adenocarcinoma cell lines was determined, demonstrating high cytotoxicity. The compound is able to induce apoptosis and a slight delay in cancer cell cycle progression, probably by its interaction with DNA and induction of double-strand pDNA cleavage, which is enhanced by oxidative mechanisms. Moreover, proteomic studies indicate that the compound induces alterations in proteins involved in cytoskeleton maintenance, cell cycle progression and apoptosis, corroborating its antiproliferative potential.

show abstract

Interaction between a potent corticosteroid drug – Dexamethasone with bovine serum albumin and human serum albumin: A fluorescence quenching and fourier transformation infrared spectroscopy study

Cited by 210 publications

References 33 publications

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Characterization of 6‐propylthiouracil and its interaction with human serum albumin on Au surface by surface‐enhanced Raman scattering

Characterization of antiproliferative potential and biological targets of a copper compound containing 4′-phenyl terpyridine

Contact Info

Product

Resources

About