Steady-State and Time-Resolved Study of the Proton-Transfer Fluorescence of 4-Hydroxy-5-azaphenanthrene in Model Solvents and in Complexes with Human Serum Albumin

1995 ◽  
Vol 99 (34) ◽  
pp. 13028-13032 ◽  
Author(s):  
Alexander Sytnik ◽  
Juan Carlos Del Valle
1998 ◽  
Vol 75 (2) ◽  
pp. 1084-1096 ◽  
Author(s):  
Kulwinder Flora ◽  
John D. Brennan ◽  
Gary A. Baker ◽  
Meagan A. Doody ◽  
Frank V. Bright

1997 ◽  
Vol 62 (11) ◽  
pp. 1815-1820 ◽  
Author(s):  
Miroslav Štěpánek ◽  
Zdeněk Pavlíček

Process of glycation of human serum albumin (HSA) by DL-glyceraldehyde was studied using steady-state and time-resolved fluorescence spectroscopy in the course of 100 h. During this period, measurements of steady-state tryptophan (Trp) and non-tryptophan (non-Trp) fluorescence of the glycated HSA were carried out, together with measurement of the non-Trp fluorescence decay and steady-state quenching using potassium iodide as a quencher. Observed changes in both Trp and non-Trp fluorescence intensity, as well as changes in non-Trp fluorescence lifetimes and quenching efficiency are explained with respect to a probable mechanism of glycation.


Biomolecules ◽  
2018 ◽  
Vol 8 (3) ◽  
pp. 78 ◽  
Author(s):  
Otávio Chaves ◽  
Maurício Tavares ◽  
Micael Cunha ◽  
Roberto Parise-Filho ◽  
Carlos Sant’Anna ◽  
...  

The interaction between the main carrier of endogenous and exogenous compounds in the human bloodstream (human serum albumin, HSA) and a potential anticancer compound (the capsaicin analogue RPF101) was investigated by spectroscopic techniques (circular dichroism, steady-state, time-resolved, and synchronous fluorescence), zeta potential, and computational method (molecular docking). Steady-state and time-resolved fluorescence experiments indicated an association in the ground state between HSA:RPF101. The interaction is moderate, spontaneous (ΔG° < 0), and entropically driven (ΔS° = 0.573 ± 0.069 kJ/molK). This association does not perturb significantly the potential surface of the protein, as well as the secondary structure of the albumin and the microenvironment around tyrosine and tryptophan residues. Competitive binding studies indicated Sudlow’s site I as the main protein pocket and molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces.


RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14335-14347 ◽  
Author(s):  
Raina Thakur ◽  
Anupam Das ◽  
Anjan Chakraborty

The interaction of human serum albumin (HSA) with liposomes made of saturated and unsaturated phosphocholines has been studied using circular dichroism (CD), steady state and time resolved fluorescence spectroscopic techniques.


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