Review: modifications of human serum albumin and their binding effect.
Human serum albumin (HSA) regulates the transport and availability of numerous chemical compounds and molecules in the blood vascular system. While previous HSA research has found that HSA interacts with specific varieties of ligands, new research efforts aim to expand HSA's ability to interact with more different drugs in order to improve the delivery of various pharmacological drugs. This review will cover fatty acid chain and posttranslational modifications of HSA that potentially modulate how HSA interacts with various pharmacological drugs, including glycation, cysteinylation, S-nitrosylation, S-transnitrosation and S-guanylation.
Philbert
P
Lee
929 E. 57 St., Chicago, Illinois USA, Zip code: 60637. Xiaoyangwu@uchicago.edu.
Xiaoyang
X
Wu
D000818:Animals; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*
D012709:Serum Albumin