Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide.

ABSTRACT: The long-acting glucagon-like peptide-1 analogue liraglutide has proven efficiency in the management of type 2 diabetes and also has beneficial effects on cardiovascular diseases. Liraglutide's protracted action highly depends on its capacity to bind to albumin via its palmitic acid part. However, in diabetes, albumin can undergo glycation, resulting in impaired drug binding. Our objective in this study was to assess the impact of human serum albumin (HSA) glycation on liraglutide affinity. Using fluorine labeling of the drug and ¹⁹F NMR, we determined HSA affinity for liraglutide in two glycated albumin models. We either glycated HSA in vitro by incubation with glucose (G25- or G100-HSA) or methylglyoxal (MGO-HSA) or purified in vivo glycated HSA from the plasma o

SUBMITTER: Gajahi Soudahome A 

PROVIDER: S-EPMC5880132 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature