Phosphate ester serum albumin affinity tags greatly improve peptide half-life in vivo

Zobel, Kerry; Koehler, Michael F. T.; Beresini, Maureen H.; Caris, Lisa D.; Combs, Daniel L.

doi:10.1016/s0960-894x(03)00209-9

Cited by 26 publications

(32 citation statements)

References 15 publications

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“…The contrast agent begins to spin much more slowly, at the rate albumin spins, causing a relaxivity gain that produces a substantially brighter signal than would be possible with freely circulating gadolinium (Table 4). 117,126–128 …”

Section: Medical Applications Based On Hsa-conjugates or Hsa-bindimentioning

confidence: 99%

Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy

2016

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Albumin is the most abundant circulating protein in plasma and has recently emerged as a versatile protein carrier for drug targeting and for improving the pharmacokinetic profile of peptide or protein based drugs. Three drug delivery technologies related to albumin have been developed, which include the coupling of low-molecular weight drugs to exogenous or endogenous albumin, conjugating bioactive proteins by albumin fusion technology (AFT), and encapsulation of drugs into albumin nanoparticles. This review article starts with a brief introduction of human serum albumin (HSA), and then summarizes the mainstream chemical strategies of developing HSA binding molecules for coupling with drug molecules. Moreover, we also concisely condense the recent progress of the most important clinical applications of HSA-binding platforms, and specify the current challenges that need to be met for a bright future of HSA-binding.

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Section: Medical Applications Based On Hsa-conjugates or Hsa-bindimentioning

confidence: 99%

Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy

2016

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“…Fibrinopeptide B has a half-life of only a few minutes in a test tube when clotting is activated (38 ). Pharmacologically, linking small peptides or proteins to carriers such as polyethylene glycol or adding tags that bind to albumin are recognized as strategies to greatly extend the circulating half-life (90,91 ). The concentrations of small peptide fragments of proteins on carrier molecules ultimately depend on several factors, including the rate of formation, the half-life of the carrier molecule, and the affinity for the carrier molecule.…”

Section: Clinical Chemistrymentioning

confidence: 99%

The MALDI-TOF Mass Spectrometric View of the Plasma Proteome and Peptidome

Hortin¹

2006

Clinical Chemistry

324

245

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“…Tumors and inflamed tissues show increased accumulation of albumin as a result of leaky capillaries and defective lymphatic drainage and this increases the fluid phase uptake that favors engulfment of abundant albumin used as a natural nitrogen and energy source. [119][120][121] The affinity for albumin determines the duration of the therapeutic effect. This phenomenon has been extensively used for the antimetabolite substance methotrexate (albumin-MTX) in treatment of renal carcinomas and rheumatoid arthritis.…”

Section: Albumin Fusion and Engineeringmentioning

confidence: 99%

The Versatile MHC Class I-related FcRn Protects IgG and Albumin from Degradation: Implications for Development of New Diagnostics and Therapeutics

Andersen

Sandlie

2009

Drug Metabolism and Pharmacokinetics

110

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The half-life of the two most abundant proteins in blood, immunoglobulin G (IgG) and serum albumin, is extraordinary (approximately 19-23 days) compared to other circulating proteins. This phenomenon secures a broad biodistribution throughout the body of both molecules. The long half-life has made IgG the natural choice for engineering of antibody based therapeutics, while albumin is used as a fusion partner for or carrier of drugs. Remarkably, the half-life of these unrelated proteins has been shown prolonged by a receptor recycling pathway mediated by a common cell bound receptor named the neonatal Fc receptor (FcRn). This review summarizes our current understanding of FcRn function and discusses its relevance for development of new IgG and albumin based therapeutics and diagnostics.

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Phosphate ester serum albumin affinity tags greatly improve peptide half-life in vivo

Cited by 26 publications

References 15 publications

Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy

Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy

The MALDI-TOF Mass Spectrometric View of the Plasma Proteome and Peptidome

The Versatile MHC Class I-related FcRn Protects IgG and Albumin from Degradation: Implications for Development of New Diagnostics and Therapeutics

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