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

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          Abstract

          Serum albumin is exposed to numerous structural modifications which affect its stability and activity. Glycation is one of the processes leading to the loss of the original properties of the albumin and physiological function disorder. In terms of long lasting states of the hyperglycemia, Advanced Glycation End-products (AGEs) are formed. AGEs are responsible for cellular and tissue structure damage that cause the appearance of a number of health consequences and premature aging. The aim of the present study was to analyze the conformational changes of serum albumin by glycation—“fructation”—using multiple spectroscopic techniques, such as absorption (UV-Vis), fluorescence (SFM), circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy and evaluate of possible alteration of binding and competition between tolbutamide (TB, a first-generation sulfonylurea oral hypoglycemic drug) and losartan (LOS, an angiotensin II receptor (AT 1) blocker used in hypertension (1st line with a coexisting diabetes)) in binding to non-glycated (HSA) and glycated (gHSA FRC) human serum albumin in high-affinity binding sites. The studies allowed us to indicate the structural alterations of human serum albumin as a result of fructose glycation. Changes in binding parameters, such as association ( K a ) or Stern-Volmer ( K S V ) constants suggest that glycation increases the affinity of TB and LOS towards albumin and affects interactions between them. The process of albumin glycation influences the pharmacokinetics of drugs, thus monitored pharmacotherapy is reasonable in the case of diabetes and hypertension polypharmacy. This information may lead to the development of more effective drug treatments based on personalized medicine for patients with diabetes. Our studies suggest the validity of monitored polypharmacy of diabetes and coexisting diseases.

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          How to study proteins by circular dichroism.

          Circular dichroism (CD) is being increasingly recognised as a valuable technique for examining the structure of proteins in solution. However, the value of many studies using CD is compromised either by inappropriate experimental design or by lack of attention to key aspects of instrument calibration or sample characterisation. In this article, we summarise the basis of the CD approach and its application to the study of proteins, and then present clear guidelines on how reliable data can be obtained and analysed.
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            The characterization of two specific drug binding sites on human serum albumin.

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              Fluorescence quenching studies with proteins.

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                Author and article information

                Journal
                Molecules
                Molecules
                molecules
                Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
                MDPI
                1420-3049
                17 December 2017
                December 2017
                : 22
                : 12
                : 2249
                Affiliations
                School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Chair and Department of Physical Pharmacy, Jagiellońska 4, Medical University of Silesia, 41-200 Sosnowiec, Poland; dpentak@ 123456sum.edu.pl (D.P.); aploch@ 123456sum.edu.pl (A.P.); jadwiga.pozycka@ 123456o2.pl (J.P.); mmaciazek@ 123456sum.edu.pl (M.M.-J.)
                Author notes
                [* ]Correspondence: aszkudlarek@ 123456sum.edu.pl ; Tel.: +48-32-364-1581
                Article
                molecules-22-02249
                10.3390/molecules22122249
                6149683
                29258218
                8382625e-74f2-43d9-a24e-8eacc2d9c869
                © 2017 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 20 November 2017
                : 15 December 2017
                Categories
                Article

                glycation,drug-drug-albumin binding,sfm,uv-vis,cd and 1h-nmr spectroscopy

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