Effect of sucrose on chemically and thermally induced unfolding of domain-I of human serum albumin: Solvation dynamics and fluorescence anisotropy study

2016 ◽  
Vol 211 ◽  
pp. 59-69 ◽  
Author(s):  
Rajeev Yadav ◽  
Bhaswati Sengupta ◽  
Pratik Sen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Anisotropy ◽  
Solvation Dynamics ◽  
Thermally Induced ◽  
Domain I

Molecular basis of the inhibition and disaggregation of thermally-induced amyloid fibrils of human serum albumin by an anti-Parkinson's drug, benserazide hydrochloride

2019 ◽  
Vol 278 ◽  
pp. 553-567 ◽  
Author(s):  
Tajalli Ilm Chandel ◽  
Aiman Masroor ◽  
Mohammad Khursheed Siddiqi ◽  
Ibrar Ahmad Siddique ◽  
Ishrat Jahan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Basis ◽  
Amyloid Fibrils ◽  
Thermally Induced

Probing Deuterium Isotope Effect on Structure and Solvation Dynamics of Human Serum Albumin

ChemPhysChem ◽  
2011 ◽  
Vol 12 (4) ◽  
pp. 814-822 ◽  
Author(s):  
Dibyendu Kumar Das ◽  
Tridib Mondal ◽  
Ujjwal Mandal ◽  
Kankan Bhattacharyya
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Isotope Effect ◽  
Solvation Dynamics ◽  
Deuterium Isotope Effect

Dynamics of Loop 1 of Domain I in Human Serum Albumin When Dissolved in Ionic Liquids

2009 ◽  
Vol 113 (38) ◽  
pp. 12825-12830 ◽  
Author(s):  
Taylor A. Page ◽  
Nadine D. Kraut ◽  
Phillip M. Page ◽  
Gary A. Baker ◽  
Frank V. Bright
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Domain I

scholarly journals Recombinant Human Serum Albumin Containing 3 Copies of Domain I, Has Significant in Vitro Antioxidative Capacity Compared to the Wild-Type

2017 ◽  
Vol 40 (10) ◽  
pp. 1813-1817 ◽  
Author(s):  
Sadaharu Matsushita ◽  
Koji Nishi ◽  
Yasunori Iwao ◽  
Yu Ishima ◽  
Hiroshi Watanabe ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antioxidative Capacity ◽  
Wild Type ◽  
Recombinant Human Serum Albumin ◽  
Domain I

scholarly journals Expression, purification and initial characterization of human serum albumin domain I and its cysteine 34

PLoS ONE ◽  
2020 ◽  
Vol 15 (10) ◽  
pp. e0240580
Author(s):  
Martina Steglich ◽  
Rodrigo Lombide ◽  
Ignacio López ◽  
Madelón Portela ◽  
Martín Fló ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Initial Characterization ◽  
Domain I

scholarly journals Human Serum Albumin Domain I Fusion Protein for Antibody Conjugation

2016 ◽  
Vol 27 (10) ◽  
pp. 2271-2275 ◽  
Author(s):  
James T. Patterson ◽  
Henry D. Wilson ◽  
Shigehiro Asano ◽  
Napon Nilchan ◽  
Roberta P. Fuller ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fusion Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
Antibody Conjugation ◽  
Domain I

Ultrafast Solvation Dynamics of Human Serum Albumin:  Correlations with Conformational Transitions and Site-Selected Recognition

2006 ◽  
Vol 110 (21) ◽  
pp. 10540-10549 ◽  
Author(s):  
Weihong Qiu ◽  
Luyuan Zhang ◽  
Oghaghare Okobiah ◽  
Yi Yang ◽  
Lijuan Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Transitions ◽  
Solvation Dynamics

Probing the binding of thioTEPA to human serum albumin using spectroscopic and molecular simulation approaches

2014 ◽  
Vol 92 (11) ◽  
pp. 1066-1073 ◽  
Author(s):  
Mohammad Mehdi Alavianmehr ◽  
Reza Yousefi ◽  
Fatemeh Keshavarz ◽  
Delara Mohammad-Aghaie
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Spherical Geometry ◽  
Free Energies ◽  
Docking Simulations ◽  
Uv Visible ◽  
Domain I ◽  
Binding Free Energies

The present work is devoted to probing the molecular interaction of N,N′,N″-triethylenethiophosphoramide (thioTEPA) with human serum albumin (HSA) using UV-visible and fluorescence spectroscopies. Further, molecular dynamics and molecular docking simulations were used to investigate the binding site of thioTEPA. The outcomes of the spectroscopic observations and also the Stern−Volmer and van’t Hoff equations were employed to determine the binding thermodynamic parameters. It was found out that the interaction of thioTEPA with HSA is enthalpy driven through a quenching mechanism that is both static and dynamic at domain I of HSA. No significant changes in the local and overall secondary structure, polarity, and hydrophobicity of HSA were observed. The low values of binding free energies and binding constants are evidence for necessary high dosage of thioTEPA in chemotherapies. These results may be attributed to the spherical geometry and steric hindrance of the free vibrating aziridinyl groups of thioTEPA.

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