First Immunoassay for Measuring Isoaspartate in Human Serum Albumin

Isoaspartate (isoAsp) is a damaging amino acid residue formed in proteins mostly as a result of spontaneous deamidation of asparaginyl residues. An association has been found between isoAsp in human serum albumin (HSA) and Alzheimer’s disease (AD). Here we report on a novel monoclonal antibody (mAb) 1A3 with excellent specificity to isoAsp in the functionally important domain of HSA. Based on 1A3 mAb, an indirect enzyme-linked immunosorbent assay (ELISA) was developed, and the isoAsp occupancy in 100 healthy plasma samples was quantified for the first time, providing the average value of (0.74 ± 0.13)%. These results suggest potential of isoAsp measurements for supplementary AD diagnostics as well as for assessing the freshness of stored donor blood and its suitability for transfusion.

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Human Serum Albumin Cys34Oxidative Modifications following Infiltration in the Carotid Atherosclerotic Plaque

Oxidative Medicine and Cellular Longevity ◽

10.1155/2014/690953 ◽

2014 ◽

Vol 2014 ◽

pp. 1-7 ◽

Cited By ~ 7

Author(s):

Antonio Junior Lepedda ◽

Angelo Zinellu ◽

Gabriele Nieddu ◽

Pierina De Muro ◽

Ciriaco Carru ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Carotid Endarterectomy ◽

Atherosclerotic Plaque ◽

Plasma Samples ◽

Carotid Atherosclerotic Plaque ◽

Sds Page ◽

Oxidative Modifications ◽

First Time

Objectives.To evaluate if the prooxidant environment present in atherosclerotic plaque may oxidatively modify filtered albumin.Methods.Fluorescein-5-maleimide labelled plasma samples and plaque extracts from 27 patients who had undergone carotid endarterectomy were analysed through nonreducing SDS-PAGE for albumin-Cys34oxidation. Furthermore, degree and pattern of S-thiolation in both circulating and plaque-filtered albumin were assayed.Results.Albumin filtered in the atherosclerotic plaque showed higher levels of Cys34oxidative modifications than the corresponding circulating form as well as different patterns of S-thiolation.Conclusions.Data indicate that the circulating albumin, once filtered in plaque, undergoes Cys34oxidative modifications and demonstrate for the first time that albumin is a homocysteine and cysteinylglycine vehicle inside the plaque environment.

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

International Journal of Molecular Sciences ◽

10.3390/ijms19102868 ◽

2018 ◽

Vol 19 (10) ◽

pp. 2868 ◽

Cited By ~ 1

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.

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Cross-reaction of antibodies to the nine-amino acid repeats ofPlasmodium falciparum antigen 11.1 with human serum albumin

European Journal of Immunology ◽

10.1002/eji.1830220214 ◽

1992 ◽

Vol 22 (2) ◽

pp. 381-385 ◽

Cited By ~ 4

Author(s):

Odile Mercereau-Puijalon ◽

Micheline Guillotte ◽

Noëlle Doyen

Keyword(s):

Amino Acid ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Cross Reaction ◽

Amino Acid Repeats ◽

Ofplasmodium Falciparum

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Spectroscopic and molecular modeling studies of human serum albumin interaction with propyl gallate

RSC Advances ◽

10.1039/c4ra11103f ◽

2014 ◽

Vol 4 (110) ◽

pp. 64559-64564 ◽

Cited By ~ 36

Author(s):

Jafar Ezzati Nazhad Dolatabadi ◽

Vahid Panahi-Azar ◽

Abolfazl Barzegar ◽

Ali Akbar Jamali ◽

Fahimeh Kheirdoosh ◽

...

Keyword(s):

Molecular Modeling ◽

Human Serum Albumin ◽

Fluorescence Quenching ◽

Serum Albumin ◽

Human Serum ◽

Propyl Gallate ◽

Fluorescence Quenching Method ◽

Molecular Modeling Studies ◽

Quenching Method ◽

First Time

For the first time, PG interaction with HSA using fluorescence quenching method, circular dichroism spectroscopy and molecular modeling was investigated.

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