Unveiling the Role of Hydrogen Bonding and g-Tensor in the Interaction of Ru-Bis-DMSO with Amino Acid Residue and Human Serum Albumin

2020 ◽  
Vol 124 (30) ◽  
pp. 6459-6474
Author(s):  
Dharitri Das ◽  
Snigdha Dutta ◽  
Dikshita Dowerah ◽  
Ramesh Chandra Deka
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Residue

The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX

2009 ◽  
Vol 7 (18) ◽  
pp. 3836 ◽  
Author(s):  
Teruyuki Komatsu ◽  
Akito Nakagawa ◽  
Stephen Curry ◽  
Eishun Tsuchida ◽  
Kenichi Murata ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protoporphyrin Ix ◽  
Heme Pocket ◽  
Iron Protoporphyrin

Efficient identification of photolabelled amino acid residues by combining immunoaffinity purification with MS: revealing the semotiadil-binding site and its relevance to binding sites for myristates in domain III of human serum albumin

2002 ◽  
Vol 363 (2) ◽  
pp. 223-232 ◽  
Author(s):  
Kohichi KAWAHARA ◽  
Akihiko KUNIYASU ◽  
Katsuyoshi MASUDA ◽  
Masaji ISHIGURO ◽  
Hitoshi NAKAYAMA
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Residue ◽  
Binding Sites ◽  
Immunoaffinity Purification ◽  
Ms Analysis ◽  
Domain Iii ◽  
Tof Ms

To identify photoaffinity-labelled amino acid residue(s), we devised an effective method utilizing immunoaffinity purification of photolabelled fragments, followed by matrix-assisted laser-desorption ionization-time of flight (MALDI-TOF) MS and nanoelectrospray ionization tandem MS (nano-ESI-MS/MS) analysis. Human serum albumin (HSA) was photolabelled with an azidophenyl derivative of semotiadil, FNAK {(+)-(R)-3,4-dihydro-2-[5-methoxy-2-[3-[N-methyl-N-[2-(3-azidophenoxy)-ethyl]amino]propoxyl]phenyl]-4-methyl-2H-1,4-benzothiazin-3-(4H)-one}, since HSA is a major binding protein for semotiadil in serum. After lysyl endopeptidase digestion, photolabelled HSA fragments were adsorbed selectively on to Sepharose beads on which an anti-semotiadil antibody was immobilized, and fractions were eluted quantitatively by 50% acetonitrile/10mM HCl. MALDI-TOF MS analysis of the eluted fraction showed that it contained two photolabelled fragments of m/z 2557.54 (major) and 1322.44 (minor), corresponding to Lys-414—Lys-432 and Ala-539—Lys-545, respectively. Further nano-ESI-MS/MS analysis revealed that Lys-414 was the photolabelled amino acid residue in fragment 414–432 and Lys-541 was a likely candidate in fragment 539–545. Based on the photolabelling results, we constructed a three-dimensional model of the FNAK—HSA complex, revealing that FNAK resides in a pocket that overlaps considerably with myristate (Myr)-binding sites, Myr-3 and −4, by comparison with crystallographic data of HSA—Myr complexes described in Curry, Mandelkow, Brick and Franks (1998) Nat. Struct. Biol. 5, 827–835. Moreover, addition of Myr increased photo-incorporation into Lys-414, whereas incorporation into Lys-541 decreased under conditions of [Myr]/[HSA]<1. Further addition of Myr, however, uniformly decreased photo-incorporation into both Lys residues. These results indicate that FNAK labelling can also be used to monitor Myr binding in domain III. An interpretation for the concomitant local conformational change of HSA is provided.

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.

scholarly journals Role of cationic carbosilane dendrons and metallic core of functionalized gold nanoparticles in their interaction with human serum albumin

2018 ◽  
Vol 118 ◽  
pp. 1773-1780 ◽  
Author(s):  
Dzmitry Shcharbin ◽  
Elzbieta Pedziwiatr-Werbicka ◽  
Tatyana Serchenya ◽  
Sylwia Cyboran-Mikolajczyk ◽  
Lena Prakhira ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Metallic Core ◽  
Functionalized Gold Nanoparticles

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
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