A novel 3D-printed centrifugal ultrafiltration method reveals in vivo glycation of human serum albumin decreases its binding affinity for zinc

Plasma proteins are covalently modified in vivo by the high-glucose conditions in the bloodstreams of people with diabetes, resulting in changes to both structure and function. Human Serum Albumin (HSA) functions as a carrier-protein in the bloodstream, binding various ligands and tightly regulating...

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Bibliographic Details
Published in:Metallomics 2020-07, Vol.12 (7), p.1036-1043
Main Authors: Jacobs, Monica J, Pinger, Cody W, Castiaux, Andre D, Maloney, Konnor J, Spence, Dana M
Format: Article
Language:English
Subjects:
Affinity
Affinity chromatography
Albumin
Binding
Bioavailability
Complications
Diabetes
Diabetes mellitus
Diabetes mellitus (insulin dependent)
Donors (electronic)
Glucose
Glycosylation
Heavy metals
Human serum albumin
In vivo methods and tests
Ligands
Maillard reaction
Mass spectrometry
Mass spectroscopy
Plasma
Plasma proteins
Proteins
Serum albumin
Structure-function relationships
Three dimensional printing
Ultrafiltration
Zinc
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Summary:Plasma proteins are covalently modified in vivo by the high-glucose conditions in the bloodstreams of people with diabetes, resulting in changes to both structure and function. Human Serum Albumin (HSA) functions as a carrier-protein in the bloodstream, binding various ligands and tightly regulating their bioavailability. HSA is known to react with glucose via the Maillard reaction, causing adverse effects on its ability to bind and deliver certain ligands, such as metals. Here, the binding between in vivo glycated HSA and zinc (Zn2+) was determined using a novel centrifugal ultrafiltration method that was developed using a 3D-printed device. This method is rapid (90 minutes), capable of high-throughput measurements (24 samples), low-cost (
ISSN:1756-5901
1756-591X
DOI:10.1039/d0mt00123f