NDLI: Functional Analysis of Recombinant Human Serum Albumin Domains for Pharmaceutical Applications

Content Provider	Springer Nature Link
Author	Matsushita, Sadaharu Isima, Yu Chuang, Victor Tuan Giam Watanabe, Hiroshi Tanase, Sumio Maruyama, Toru Otagiri, Masaki
Copyright Year	2004
Abstract	Purpose. Functional analysis of the three recombinant human serum albumin (rHSA) domains and their potential as stand-alone proteins for use as drug delivery protein carriers. Methods. Protein structure was examined by fluorescence and CD spectroscopy. Ligand binding was estimated by ultrafiltration. Antioxidant activity was estimated by measuring the quenching of dihydrorhodamine 123. Esterase-like activity and enolase-like activity were estimated from the rate of hydrolysis of p-nitrophenyl acetate and conversion of dihydrotestosterone from the 3-keto to 3-enol form, respectively. The domains of human serum albumin (HSA) were radiolabeled with $^{111}$In to evaluate their pharmacokinetics. Results. The ligand binding ability of subsites Ia and Ib could not be detected in domain II. However, the binding of ligands to subsite Ic and site II were preserved in domain II and domain III, respectively. Domain III retained about 45% of its esterase-like activity, and weaker esterase-like activity was also observed in domain I. All domains showed low enolase-like activity in a pH 7.4 phosphate buffer, but domain II had higher activity in a pH 9.2 carbonate buffer. Domain I exhibited antioxidant activity comparable to that of rHSA. All three of the $^{111}$In-radiolabeled domains were rapidly eliminated from HSA, with high accumulation in the kidneys. Conclusion. Domain I of HSA has great potential for further development as a drug delivery protein carrier, due to its favorable properties and the presence of a free cysteine residue.
Starting Page	1924
Ending Page	1932
Page Count	9
File Format	PDF
ISSN	07248741
Journal	Pharmaceutical Research
Volume Number	21
Issue Number	10
e-ISSN	1573904X
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2004-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pharmacology/Toxicology Pharmacy Biochemistry Medical Law Biomedical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Pharmacology Molecular Medicine Pharmacology (medical) Biotechnology Pharmaceutical Science

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