Pharmaceutical Aspects of the Recombinant Human Serum Albumin Dimer: Structural Characteristics, Biological Properties, and Medical Applications

Taguchi, Kazuaki; Chuang, Victor Tuan Giam; Maruyama, Toru; Otagiri, Masaki

doi:10.1002/jps.23181

Cited by 54 publications

(42 citation statements)

References 93 publications

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“…Still, the use of HSA solutions instead of alternative fluids is controversial [59–61]. HSA is also of pharmaceutical interest as a drug carrier [62], and several HSA-based drugs have received market approval or are in clinical development [63]. The availability of recombinant HSA has been essential for broadening the pharmaceutical applications of the protein [64–66].…”

Section: Hsa Has Several Functions Including the Binding Of Exogenousmentioning

confidence: 99%

The thiol pool in human plasma: The central contribution of albumin to redox processes

Turell

Radí

Álvarez

2013

Free Radical Biology and Medicine

592

521

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The plasma compartment has particular features regarding the nature and concentration of low and high molecular weight thiols and oxidized derivatives. Plasma is relatively poor in thiol-based antioxidants; thiols are in lower concentrations than in cells and mostly oxidized. The different thiol-disulfide pairs are not in equilibrium and the steady-state concentrations of total thiols as well as reduced versus oxidized ratios are maintained by kinetic barriers, including the rates of reactions and transport processes. The single thiol of human serum albumin (HSA-SH) is the most abundant plasma thiol. It is an important target for oxidants and electrophiles due to its reactivity with a wide variety of species and its relatively high concentration. A relatively stable sulfenic (HSA-SO3H) acid can be formed in albumin exposed to oxidants. Plasma increases in mixed disulfides (HSA-SSR) or in sulfinic (HSA-SO2H) and sulfonic (HSA-SO3H) acids are associated with different pathologies and may constitute biomarkers of the antioxidant role of the albumin thiol. In this work we provide a critical review of the plasma thiol pool with a focus on human serum albumin.

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Section: Hsa Has Several Functions Including the Binding Of Exogenousmentioning

confidence: 99%

The thiol pool in human plasma: The central contribution of albumin to redox processes

Turell

Radí

Álvarez

2013

Free Radical Biology and Medicine

592

521

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“…We previously reported HSA dimer prepared by cross‐linking two HSA molecules with 1,6‐bis(maleimido)hexane (BMH)[8] showed superior plasma retention property compared with HSA monomer in the doxorubicin‐induced nephrotic rat model [9]. In addition, the length of BMH seems to be sufficiently long (16.1 Å), permitting HSA dimer to preserve the structural properties of native HSA monomer including ligand binding capacity and blood compatibility [8,10]. These evidence had led us to hypothesize that HSA dimer produced from two HSA molecules chemically linked with BMH has the potential as a plasma‐retaining agent of antidiabetic drugs, such as fatty acid conjugated insulin analogues and GLP‐1 receptor agonist, for treating hypoalbunemia under diabetic nephropathy condition.…”

Section: Introductionmentioning

confidence: 99%

“…[9] In addition, the length of BMH seems to be sufficiently long (16.1 Å), permitting HSA dimer to preserve the structural properties of native HSA monomer including ligand binding capacity and blood compatibility. [8,10] These evidence had led us to hypothesize that HSA dimer produced from two HSA molecules chemically linked with BMH has the potential as a plasmaretaining agent of antidiabetic drugs, such as fatty acid conjugated insulin analogues and GLP-1 receptor agonist, for treating hypoalbunemia under diabetic nephropathy condition. A rat model of diabetic nephropathy induced by treatment with streptozotocin (STZ) was used to evaluate the pharmacokinetic properties of HSA monomer and HSA dimer.…”

Section: Introductionmentioning

confidence: 99%

Cross-linked human serum albumin dimer has the potential for use as a plasma-retaining agent for the fatty acid-conjugated antidiabetic drugs

Taguchi

Chuang

Yamasaki

et al. 2015

Journal of Pharmacy and Pharmacology

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“…HSA has been explored as a drug carrier due to its availability, biocompatibility, low toxicity, and minimal to none immunogenicity [24]. With unique and stable structure, albumin is well suited as a protein scaffold to be genetically engineered for novel functionalities.…”

Section: Construction Of Albumin Fusion Proteinsmentioning

confidence: 99%

Recombinant Human Serum Albumin Fusion Proteins and Novel Applications in Drug Delivery and Therapy

Rogers¹,

Dong²,

Li³

et al. 2015

CPD

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Fusion proteins have been well-studied and widely applied in biopharmaceutics. Albumin fusion proteins are simple to construct, easy to purify, and stable to formulate. One main application of fusion protein is to extend the plasma half-life of therapeutic proteins and peptides. Albiglutide for diabetes treatment is the first albumin fusion protein drug approved by FDA. Balugrastim and other albumin fusion proteins have been evaluated in clinical trials. Taking advantage of the physiological functions of albumin, albumin fusion proteins can also been applied to act on an essential intracellular target and carry fatty acid-modified drugs. This novel approach makes it possible to co-deliver two different types of drug to one tumor cell for synergistic cytotoxicity.

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Pharmaceutical Aspects of the Recombinant Human Serum Albumin Dimer: Structural Characteristics, Biological Properties, and Medical Applications

Cited by 54 publications

References 93 publications

The thiol pool in human plasma: The central contribution of albumin to redox processes

The thiol pool in human plasma: The central contribution of albumin to redox processes

Cross-linked human serum albumin dimer has the potential for use as a plasma-retaining agent for the fatty acid-conjugated antidiabetic drugs

Recombinant Human Serum Albumin Fusion Proteins and Novel Applications in Drug Delivery and Therapy

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