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Human serum albumin binders: A piggyback ride for long-acting therapeutics

DRUG DISCOVERY TODAY (2023)

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Florencio Zaragoza

Summary: An increasing number of drugs that consist of a therapeutic peptide or protein linked to an albumin-binding structure are being approved. In this perspective, the pharmacokinetic data of currently marketed drugs of this type will be presented. Acylation with fatty acids or fatty a,?-dicarboxylic acids has been used successfully to prepare long-acting analogs of insulin, GLP-1, and other peptides but not of larger proteins. With a tetrazole-sulfonylamide fatty acid bioisostere, it has now been possible to prepare a long-acting analog of human growth hormone (191 amino acids), which is suitable for once-weekly administration.

JOURNAL OF MEDICINAL CHEMISTRY (2023)

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Albumin-binding DARPins as scaffold improve the hypoglycemic and anti-obesity effects of exendin-4 in vivo

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Summary: Researchers synthesized four new GLP-1R agonists by genetically fusing Ex to HSA-binding ankyrin repeat proteins (DARPins) and found that these Ex-DARPin fusion proteins had stable structures and long half-lives. The fusion proteins showed effectiveness in lowering blood glucose, reducing body weight, and improving the survival of pancreatic islets in mice. These long-acting Ex-DARPin fusion proteins hold promise as potential therapeutic agents for diabetes and obesity.

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Summary: In this study, a novel small biological molecule, izokibep, was developed using Affibody technology to inhibit IL-17A signaling. Preclinical studies showed that izokibep selectively inhibits human IL-17A with superior potency and efficacy compared to anti-IL-17A mAbs. Phase 1 clinical trials demonstrated the safety and efficacy of izokibep in treating psoriasis.

MABS (2023)

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TRYBE®: an Fc-free antibody format with three monovalent targeting arms engineered for long in vivo half-life

Emma Dave et al.

Summary: TrYbe (R) is an Fc-free therapeutic antibody format that can engage up to three targets simultaneously and has a long half-life in vivo due to albumin binding. The format is conformationally flexible and has favorable 'reach' properties. By co-targeting soluble and cell surface antigens, the broad functionality of the format is demonstrated. TrYbes (R) are manufactured using standard mammalian cell culture and protein A affinity capture processes and have high concentrations and favorable drug-like properties. The unique functionality and developability of TrYbe (R) make it a promising multi-specific antibody fragment format for antibody therapy.

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Serum albumin binding knob domains engineered within a VH framework III bispecific antibody format and as chimeric peptides

Ralph Adams et al.

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Daham Kim et al.

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Hans Helleberg et al.

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Effective GH Replacement With Once-weekly Somapacitan vs Daily GH in Children with GHD: 3-year Results From REAL 3

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Chang Liu et al.

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Human and Mouse Cross-Reactive Albumin-Binding Helix-Loop- Helix Peptide Tag for Prolonged Bioactivity of Therapeutic Proteins

Yuto Nakatani et al.

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MOLECULAR PHARMACEUTICS (2022)

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Nadine Michot et al.

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IZOKIBEP (ABY-035) IN PATIENTS WITH ACTIVE PSORIATIC ARTHRITIS-16-WEEK RESULTS FROM A PHASE 2 STUDY

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Hanine Rafidi et al.

Summary: Advances in antibody engineering have provided new opportunities for biologic therapies, and understanding the impact of structural factors on antibody distribution properties is crucial. This study evaluated the effect of antibody size on systemic pharmacokinetics and tissue distribution. The results showed that circulating antibody had the greatest contribution to total uptake in early time points and highly vascularized tissues. Tissue interstitial pharmacokinetics largely mirrored serum exposure profiles, except for non-FcRn-binding molecules which showed changing interstitial:serum ratios over time. Additionally, the study measured concentration-time profiles of intact and catabolized molecules, revealing that IgG-HAHQ had the highest catabolism levels.

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Albumin-binding domain extends half-life of glucagon-like peptide-1

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Prediction of Half-Life Extension of Peptides via Serum Albumin Binding: Current Challenges

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Summary: The development of peptide therapeutics has increased significantly in recent decades, with serum albumin binding as a key approach to extend the half-life of peptide drugs. Challenges in quantitative prediction for humans remain, but a quantitative model integrating pharmacokinetic concepts and albumin binding has shown promising results in correlating predicted and observed values. Further development of quantitative models is necessary for predicting half-life accurately.

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Small Bispecific Affinity Proteins for Simultaneous Target Binding and Albumin-Associated Half-Life Extension

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