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Formation of Products similar to Advanced Glycation End products (SAGEs) and Binding Affinities between Keto Acids with Human Serum Albumin
Author(s) -
Cai Ang,
Tang Xiaodan,
Liu Weixi,
Ma Hang,
Dain Joel A.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.05302
Subject(s) - chemistry , isothermal titration calorimetry , glycation , levulinic acid , human serum albumin , affinities , biochemistry , metabolism , albumin , binding affinities , stereochemistry , catalysis , receptor
Children who have the diabetic ketoacidosis may suffer from cognitive decline. It believes that the cognitive decline is related to carbohydrates metabolism. Keto acids (KAs) play significant roles in biological pathways related to carbohydrates metabolism. Although we have reported that KAs (pyruvic acid, α‐ketoglutaric acid, levulinic acid, and oxaloacetic acid) can react with human serum albumin (HSA) and form similar to Advanced Glycation End products (SAGEs), to be more important, the formation of the SAGEs and binding affinities of KAs with HSA remains unclear. Hence, we evaluated four keto acids including pyruvic acid, α‐ketoglutaric acid, levulinic acid, and oxaloacetic acid for their SAGEs formation and binding affinities of them with HSA. KAs were incubated with HSA at 37 °C for seven days and the formation of SAGEs were measured by visible, fluorescence, and circular dichroism (CD) stability assays, respectively. Pyruvic acid and α‐ketoglutaric acid did not induce the formation of SAGEs while levulinic acid and oxaloacetic increased the formation of SAGEs compared to the control group. MALDI‐TOF was used to provide critical insights of KAs induced formation of SAGEs. Kinetics and binding affinity determination between KAs and HSA were performed by surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC).