Literature DB >> 28526195

Alteration of human serum albumin binding properties induced by modifications: A review.

Małgorzata Maciążek-Jurczyk1, Agnieszka Szkudlarek2, Mariola Chudzik2, Jadwiga Pożycka2, Anna Sułkowska3.   

Abstract

Albumin, a major transporting protein in the blood, is the main target of modification that affects the binding of drugs to Sudlow's site I and II. These modification of serum protein moderates its physiological function, and works as a biomarker of some diseases. The main goal of the paper was to explain the possible alteration of human serum albumin binding properties induced by modifications such as glycation, oxidation and ageing, their origin, methods of evaluation and positive and negative meaning described by significant researchers.
Copyright © 2017 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Ageing; Albumin; Glycation; Modification; Oxidation

Mesh:

Substances:

Year:  2017        PMID: 28526195     DOI: 10.1016/j.saa.2017.05.023

Source DB:  PubMed          Journal:  Spectrochim Acta A Mol Biomol Spectrosc        ISSN: 1386-1425            Impact factor:   4.098


  13 in total

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4.  In Vitro Investigation of the Interaction of Tolbutamide and Losartan with Human Serum Albumin in Hyperglycemia States.

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

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Review 9.  Oxidized Albumin as a Mediator of Kidney Disease.

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10.  Albumin-binding tag derived Exendin-4 analogue for treating hyperglycemia and diabetic complications.

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