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Glycation alters ligand binding, enzymatic, and pharmacological properties of human albumin


Reference:

Baraka-Vidot, J., Planesse, C., Meilhac, O., Militello, V., Van Den Elsen, J., Bourdon, E. and Rondeau, P., 2015. Glycation alters ligand binding, enzymatic, and pharmacological properties of human albumin. Biochemistry, 54 (19), pp. 3051-3062.

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http://dx.doi.org/10.1021/acs.biochem.5b00273

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Abstract

Albumin, the major circulating protein in blood plasma, can be subjected to an increased level of glycation in a diabetic context. Albumin exerts crucial pharmacological activities through its drug binding capacity, i.e., ketoprofen, and via its esterase-like activity, allowing the conversion of prodrugs into active drugs. In this study, the impact of the glucose-mediated glycation on the pharmacological and biochemical properties of human albumin was investigated. Aggregation product levels and the redox state were quantified to assess the impact of glycation-mediated changes on the structural properties of albumin. Glucose-mediated changes in ketoprofen binding properties and esterase-like activity were evaluated using fluorescence spectroscopy and p-nitrophenyl acetate hydrolysis assays, respectively. With the exception of oxidative parameters, significant dose-dependent alterations in biochemical and functional properties of in vitro glycated albumin were observed. We also found that the dose-dependent increase in levels of glycation and protein aggregation and average molecular mass changes correlated with a gradual decrease in the affinity of albumin for ketoprofen and its esterase-like property. In parallel, significant alterations in both pharmacological properties were also evidenced in albumin purified from diabetic patients. Partial least-squares regression analyses established a significant correlation between glycation-mediated changes in biochemical and pharmacological properties of albumin, highlighting the important role for glycation in the variability of the drug response in a diabetic situation.

Details

Item Type Articles
CreatorsBaraka-Vidot, J., Planesse, C., Meilhac, O., Militello, V., Van Den Elsen, J., Bourdon, E. and Rondeau, P.
DOI10.1021/acs.biochem.5b00273
Related URLs
URLURL Type
http://www.scopus.com/inward/record.url?scp=84929577149&partnerID=8YFLogxKUNSPECIFIED
DepartmentsFaculty of Science > Biology & Biochemistry
Research CentresCentre for Sustainable Chemical Technologies
RefereedYes
StatusPublished
ID Code44995

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