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

Metallomics ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 1036-1043 ◽  
Author(s):  
Monica J. Jacobs ◽  
Cody W. Pinger ◽  
Andre D. Castiaux ◽  
Konnor J. Maloney ◽  
Dana M. Spence
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Glucose ◽  
Plasma Proteins ◽  
Structure And Function ◽  
3D Printed ◽  
And Function ◽  
Centrifugal Ultrafiltration

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.

scholarly journals Influence of aqueous extracts of urban airborne particulate matter on the structure and function of human serum albumin

2020 ◽  
Vol 263 ◽  
pp. 114667 ◽  
Author(s):  
Olga Mazuryk ◽  
Przemysław Gajda-Morszewski ◽  
Monika Flejszar ◽  
Przemysław Łabuz ◽  
Rudi van Eldik ◽  
...  
Keyword(s):  
Particulate Matter ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Airborne Particulate Matter ◽  
Structure And Function ◽  
Aqueous Extracts ◽  
Airborne Particulate ◽  
And Function

scholarly journals Oral branched-chain amino acid granules improve structure and function of human serum albumin in cirrhotic patients

2016 ◽  
Vol 52 (6) ◽  
pp. 754-765 ◽  
Author(s):  
Hiroko Setoyama ◽  
Motohiko Tanaka ◽  
Kohei Nagumo ◽  
Hideaki Naoe ◽  
Takehisa Watanabe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structure And Function ◽  
Branched Chain Amino Acid ◽  
Cirrhotic Patients ◽  
Branched Chain ◽  
And Function

scholarly journals Understanding the effects of two bound glucose in Sudlow site I on structure and function of human serum albumin: theoretical studies

2016 ◽  
Vol 35 (4) ◽  
pp. 781-790 ◽  
Author(s):  
Tadsanee Awang ◽  
Nuttapon Wiriyatanakorn ◽  
Patchreenart Saparpakorn ◽  
Deanpen Japrung ◽  
Prapasiri Pongprayoon
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structure And Function ◽  
Theoretical Studies ◽  
And Function

Investigations on the effects of Cu2+ on the structure and function of human serum albumin

Luminescence ◽  
2015 ◽  
Vol 31 (2) ◽  
pp. 557-564 ◽  
Author(s):  
Mingyang Jing ◽  
Rutao Liu ◽  
Wenbao Yan ◽  
Xuejie Tan ◽  
Yadong Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structure And Function ◽  
And Function

Influence of Human Serum Albumin Glycation on the Binding Affinities for Natural Flavonoids

2019 ◽  
Vol 17 (1) ◽  
pp. 806-812
Author(s):  
Liangliang Liu ◽  
Yi Liu ◽  
Aiping Xiao ◽  
Shiyong Mei ◽  
Yixi Xie
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Small Molecules ◽  
Human Body ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fluorescence Spectra ◽  
Binding Affinities ◽  
Dietary Flavonoids

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.

In vitro and in vivo antitubercular activity of benzothiazinone-loaded human serum albumin nanocarriers designed for inhalation

2020 ◽  
Vol 328 ◽  
pp. 339-349 ◽  
Author(s):  
Ayasha Patel ◽  
Natalja Redinger ◽  
Adrian Richter ◽  
Arcadia Woods ◽  
Paul Robert Neumann ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antitubercular Activity

An effective and safe treatment strategy for rheumatoid arthritis based on human serum albumin and Kolliphor® HS 15

Nanomedicine ◽  
2019 ◽  
Vol 14 (16) ◽  
pp. 2169-2187 ◽  
Author(s):  
Ting Gong ◽  
Pei Zhang ◽  
Caifeng Deng ◽  
Yu Xiao ◽  
Tao Gong ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Therapeutic Strategy ◽  
Inflammatory Cell ◽  
In Vivo Studies ◽  
Targeting Ability

Aim: We aimed to construct human serum albumin-Kolliphor® HS 15 nanoparticles (HSA-HS15 NPs) to overcome the limitations in targeted therapy for rheumatoid arthritis (RA) and enhance the safety of drug-loaded HSA NPs. Methodology: Celastrol (CLT)-loaded HSA-HS15 NPs were prepared and the properties were adequately investigated; the treatment effect were evaluated in RA rats; in vitro and in vivo studies were performed to explain the mechanism. Results: CLT-HSA-HS15 NPs had remarkable treatment ability and enhanced safety in the treatment of RA compared with free CLT and CLT-HSA NPs. Conclusion: HSA-HS15 NPs could be a safe and efficient therapeutic strategy for the treatment of RA, because of the inflammatory targeting ability of albumin, the added HS15 and ELVIS effect (extravasation through leaky vasculature followed by inflammatory cell-mediated sequestration) of nanoparticles.

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