albumin - publications

Predict more albumin - ligand interactions now!

1. J Pharm Sci. 2012 Apr 4. doi: 10.1002/jps.23143. [Epub ahead of print]

S-guanylation of human serum albumin is a unique posttranslational modification
and results in a novel class of antibacterial agents.

Ishima Y, Hoshino H, Shinagawa T, Watanabe K, Akaike T, Sawa T, Kragh-Hansen U,
Kai T, Watanabe H, Maruyama T, Otagiri M.

Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences,
Kumamoto University, Kumamoto 862-0973, Japan; Center for Clinical Pharmaceutical
Science, Kumamoto University, Kumamoto, Japan.

8-Nitroguanosine 3',5'-cyclic monophosphate (8-nitro-cGMP) is a nitric oxide
metabolite and an important second messenger. 8-Nitro-cGMP reacts with sulfhydryl
groups forming a novel posttranslational modification, namely, S-guanylation. In
this work, we found, by using a quantitative competition enzyme-linked
immunosorbent assay procedure, that S-guanylated human serum albumin (S-cGMP-HSA)
is a component of normal plasma, and that hemodialysis patients decrease its
concentration, on an average, from 68 to 34 nM. End-stage renal disease is often
accompanied by septicemia, and we found that S-cGMP-HSA possesses an in vitro
antibacterial effect with half maximal inhibitory concentration of approximately
2 μM against Escherichia coli American Type Culture Collection. Our findings
indicate that S-cGMP-HSA can be regarded as an endogenous antibacterial agent in
healthy conditions and as a useful new class of antibacterial agents with a
circulation time sufficient for in vivo biological activity. The clinical
development of S-cGMP-HSA as a safe and strong antibacterial agent arisen from
endogenous posttranslational modification would be expected. © 2012 Wiley
Periodicals, Inc. and the American Pharmacists Association J Pharm Sci.

Copyright © 2012 Wiley Periodicals, Inc.

PMID: 22488009 [PubMed - as supplied by publisher]