scholarly journals Polyallylamine hydrochloride coating enhances the fluorescence emission of Human Serum Albumin encapsulated gold nanoclusters

2018 ◽  
Vol 187 ◽  
pp. 131-135 ◽  
Author(s):  
Ben Allan Russell ◽  
Barbara Jachimska ◽  
Yu Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gold Nanoclusters ◽  
Fluorescence Emission ◽  
Polyallylamine Hydrochloride

scholarly journals Human serum albumin encapsulated gold nanoclusters: effects of cluster synthesis on natural protein characteristics

2016 ◽  
Vol 4 (42) ◽  
pp. 6876-6882 ◽  
Author(s):  
B. A. Russell ◽  
B. Jachimska ◽  
I. Kralka ◽  
P. A. Mulheran ◽  
Y. Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gold Nanoclusters ◽  
Physiochemical Properties ◽  
Natural Protein

The differences in the physiochemical properties between native Human Serum Albumin (HSA) and HSA encapsulated gold nanoclusters (HSA-AuNCs) are characterised.

scholarly journals Probing the Sudlow binding site with warfarin: how does gold nanocluster growth alter human serum albumin?

2016 ◽  
Vol 18 (33) ◽  
pp. 22874-22878 ◽  
Author(s):  
B. A. Russell ◽  
P. A. Mulheran ◽  
D. J. S. Birch ◽  
Y. Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Gold Nanoclusters ◽  
Drug Binding ◽  
Gold Nanocluster ◽  
Drug Binding Site ◽  
Major Drug

Gold Nanoclusters (AuNCs) synthesised using Human Serum Albumin (HSA) as a stable scaffold are shown to modify the major drug binding site, Sudlow site I. Upon AuNC nucleation within HSA, warfarin was observed to no longer bind to Sudlow I, remaining free in solution.

scholarly journals Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

2017 ◽  
Vol 5 (1) ◽  
pp. 48-59
Author(s):  
Alla Yegorova ◽  
Inna Leonenko ◽  
Yulia Scrypynets ◽  
Georgy Maltsev ◽  
Valery Antonovich ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Average Distance ◽  
Antiviral Drug ◽  
Fluorescence Emission ◽  
Resonance Energy ◽  
Spectroscopic Studies ◽  
Excitation Wavelength

Under physiological conditions, in vitro interaction between the antiviral drug 2,7-bis[2-(diethylamino)ethoxy]-9-fluorenone dihydrochloride (Tilorone, TIL) and human serum albumin (HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K and 313 K) by fluorescence emission spectroscopy. TIL showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant is estimated as KA =7.19× 104L·mol-1 at 298 K. The enthalpy change (ΔHº) and entropy change (ΔSº) were derived to be negative values. A value of 1.63 nm for the average distance r between TIL (acceptor) and tryptophan residues of HSA (donor) was derived from the fluorescence resonance energy transfer.

DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE

2013 ◽  
Vol 08 (01n02) ◽  
pp. 59-71
Author(s):  
G. REZAEI BEHBAHANI ◽  
M. SHALBAFAN ◽  
N. GHEIBI ◽  
L. BARZEGAR ◽  
H. REZAEI BEHBAHANI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Tertiary Structure ◽  
Fluorescence Emission ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Spectroscopic Methods ◽  
Irreversible Denaturation

Cerium (III) Chloride-induced conformational changes of human serum albumin, HSA, in phosphate buffer, 10 mM at pH 7.4 was investigated, using isothermal titration calorimetry (ITC), UV and fluorescence emission spectroscopic methods. The results indicate that CeCl3, Ce3+, induces irreversible denaturation of the HSA structure. The UV absorption intensity of HSA + Ce3+ shows a slight blueshift in the absorbance wavelength with increasing Ce3+ concentration. The fluorescence intensity was increased regularly and a slight redshift was observed in the emission wavelength. The HSA + Ce3+ complex quenches the fluorescence of HSA and changes the microenvironment of tryptophan residue. The emission intensity increases suggesting the loss of the tertiary structure of HSA. The results obtained from the ITC data are in agreement with the spectroscopic methods. The strong negative cooperativity of Ce3+ binding with HSA (Table 1) recovered from the extended solvation model, indicates that HSA has been denatured as a result of its interaction with Ce3+ ions.

scholarly journals Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

2020 ◽  
Vol 11 (2) ◽  
pp. 145-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Clinical Medicine ◽  
Fluorescence Emission ◽  
Binding Constants ◽  
Binding Interaction ◽  
Binding Ability ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.

scholarly journals New copper(ii) complexes of the anti-inflammatory drug mefenamic acid: a concerted study including synthesis, physicochemical characterization and their biological evaluation

RSC Advances ◽  
2016 ◽  
Vol 6 (91) ◽  
pp. 88546-88558 ◽  
Author(s):  
Raj Pal Sharma ◽  
Santosh Kumar ◽  
Paloth Venugopalan ◽  
Valeria Ferretti ◽  
Alketa Tarushi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Mefenamic Acid ◽  
Emission Spectroscopy ◽  
Physicochemical Characterization ◽  
Fluorescence Emission ◽  
Biological Evaluation ◽  
Inflammatory Drug ◽  
Fluorescence Emission Spectroscopy

The interaction of three newly synthesized copper(ii) mefenamate complexes with bovine/human serum albumin was studied by fluorescence emission spectroscopy.

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