Battle of GLP-1 delivery technologies

Тип публикации: статья из журнала

Год издания: 2018

Идентификатор DOI: 10.1016/j.addr.2018.07.009

Ключевые слова: Albumin fusion, Exenatide, Fatty acid conjugate, Fc fusion, GLP-1 receptor agonist, Half-life, Peptide delivery, Pharmacokinetics

Аннотация: Glucagon-like peptide-1 receptor agonists (GLP-1 RAs) belong to an important therapeutic class for treatment of type 2 diabetes. Six GLP-1 RAs, each utilizing a unique drug delivery strategy, are now approved by the Food and Drug Administration (FDA) and additional, novel GLP-1 RAs are still under development, making for a crowded marketplace and fierce competition among the manufacturers of these products. As rapid elimination is a major challenge for clinical application of GLP-1 RAs, various half-life extension strategies have been successfully employed including sequential modification, attachment of fatty-acid to peptide, fusion with human serum albumin, fusion with the fragment crystallizable (Fc) region of a monoclonal antibody, sustained drug delivery systems, and PEGylation. In this review, we discuss the scientific rationale of the various half-life extension strategies used for GLP-1 RA development. By analyzing and comparing different approved GLP-1 RAs and those in development, we focus on assessing how half-life extending strategies impact the pharmacokinetics, pharmacodynamics, safety, patient usability and ultimately, the commercial success of GLP-1 RA products. We also anticipate future GLP-1 RA development trends. Since similar drug delivery strategies are also applied for developing other therapeutic peptides, we expect this case study of GLP-1 RAs will provide generalizable concepts for the rational design of therapeutic peptides products with extended duration of action. © 2018 Elsevier B.V.

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Издание

Журнал: Advanced Drug Delivery Reviews

ISSN журнала: 0169409X

Издатель: Elsevier B.V.

Авторы

  • Yu M. (Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States)
  • Benjamin M.M. (Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States)
  • Srinivasan S. (Amneal Pharmaceuticals, 50 Horseblock Rd, Brookhaven, NY, United States)
  • Morin E.E. (Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States)
  • Shishatskaya E.I. (Siberian Federal University, 79 Svobodnuy Ave, Krasnoyarsk, Russian Federation, Institute of Biophysics SBRAS, 50 Akademgorodok, Russian Federation)
  • Schwendeman S.P. (Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States, Biointerfaces Institute, NCRC, 2800 Plymouth Rd, Ann Arbor, MI, United States, Department of Biomedical Engineering, 2200 Bonisteel Blvd, Ann Arbor, MI, United States)
  • Schwendeman A. (Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, 428 Church St, Ann Arbor, MI, United States, Biointerfaces Institute, NCRC, 2800 Plymouth Rd, Ann Arbor, MI, United States)

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