Peculiarities of Dansyl Amino Acid Enantioselectivity Using Human Serum Albumin as a Chiral Selector

1998 ◽  
Vol 36 (2) ◽  
pp. 97-103 ◽  
Author(s):  
E. Peyrin ◽  
Y. C. Guillaume ◽  
C. Guinchard
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chiral Selector ◽  
Dansyl Amino Acid

scholarly journals Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation

2018 ◽  
Vol 19 (10) ◽  
pp. 2868 ◽  
Author(s):  
Luiza Bertozo ◽  
Ernesto Tavares Neto ◽  
Leandro Oliveira ◽  
Valdecir Ximenes
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Energy ◽  
Score Function ◽  
Oxidation Products ◽  
Amino Acid Residues ◽  
Computational Investigation ◽  
A Current

Human serum albumin (HSA) is a target for reactive oxygen species (ROS), and alterations of its physiological functions caused by oxidation is a current issue. In this work, the amino-acid residues Trp-214 and Lys-199, which are located at site I of HSA, were experimentally and computationally oxidized, and the effect on the binding constant with phenylbutazone was measured. HSA was submitted to two mild oxidizing reagents, taurine monochloramine (Tau-NHCl) and taurine dibromamine (Tau-NBr2). The oxidation of Trp-214 provoked spectroscopic alterations in the protein which were consistent with the formation of N′-formylkynurenine. It was found that the oxidation of HSA by Tau-NBr2, but not by Tau-NHCl, provoked a significant increase in the association constant with phenylbutazone. The alterations of Trp-214 and Lys-199 were modeled and simulated by changing these residues using the putative oxidation products. Based on the Amber score function, the interaction energy was measured, and it showed that, while native HSA presented an interaction energy of −21.3 kJ/mol, HSA with Trp-214 altered to N′-formylkynurenine resulted in an energy of −28.4 kJ/mol, and HSA with Lys-199 altered to its carbonylated form resulted in an energy of −33.9 kJ/mol. In summary, these experimental and theoretical findings show that oxidative alterations of amino-acid residues at site I of HSA affect its binding efficacy.

Fast enantiomeric separation of propranolol by affinity capillary electrophoresis using human serum albumin as chiral selector: application to quality control of pharmaceuticals

2004 ◽  
Vol 507 (2) ◽  
pp. 171-178 ◽  
Author(s):  
Juan José Martı́nez-Pla ◽  
Yolanda Martı́n-Biosca ◽  
Salvador Sagrado ◽  
Rosa Marı́a Villanueva-Camañas ◽  
Marı́a José Medina-Hernández
Keyword(s):  
Quality Control ◽  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Enantiomeric Separation ◽  
Chiral Selector ◽  
Affinity Capillary Electrophoresis

scholarly journals Oral branched-chain amino acid granules improve structure and function of human serum albumin in cirrhotic patients

2016 ◽  
Vol 52 (6) ◽  
pp. 754-765 ◽  
Author(s):  
Hiroko Setoyama ◽  
Motohiko Tanaka ◽  
Kohei Nagumo ◽  
Hideaki Naoe ◽  
Takehisa Watanabe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structure And Function ◽  
Branched Chain Amino Acid ◽  
Cirrhotic Patients ◽  
Branched Chain ◽  
And Function

The binding affinity of amino acid–protein: hydroxyproline binding site I on human serum albumin

2012 ◽  
Vol 10 (41) ◽  
pp. 8314 ◽  
Author(s):  
Ximin Zhou ◽  
Wenjuan Lü ◽  
Li Su ◽  
Yalei Dong ◽  
Qianfeng Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Affinity ◽  
Acid Protein ◽  
Amino Acid Protein

Binding behavior of amino acid conjugates of indole-3-acetic acid to immobilized human serum albumin

2007 ◽  
Vol 1154 (1-2) ◽  
pp. 240-249 ◽  
Author(s):  
Ana Tomašić ◽  
Branimir Bertoša ◽  
Sanja Tomić ◽  
Milan Šoškić ◽  
Volker Magnus
Keyword(s):  
Acetic Acid ◽  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Conjugates ◽  
Binding Behavior ◽  
Indole 3 Acetic Acid

Site-directed mutagenesis studies of human serum albumin define tryptophan at amino acid position 214 as the principal site for nitrosation

2002 ◽  
Vol 9 (1) ◽  
pp. 47-58 ◽  
Author(s):  
Krishna Harohalli ◽  
Charles E. Petersen ◽  
Chung-Eun Ha ◽  
Jimmy B. Feix ◽  
Nadhipuram V. Bhagavan
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Position ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Amino Acid Sequence ofN-Terminal Peptide of Normal Human Serum Albumin

1971 ◽  
Vol 18 (3) ◽  
pp. 137-144 ◽  
Author(s):  
C.S. Liu ◽  
T. B. Shih ◽  
M.H. Hsin ◽  
R. Q. Blackwell
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Amino Acid Sequence ◽  
Serum Albumin ◽  
Human Serum ◽  
Normal Human Serum ◽  
Normal Human
Sign in / Sign up

Export Citation Format

Share Document