Live long and active: Polypeptide-mediated assembly of antibody variable fragments
| Autor: | Minchang Choi, J. Andrew MacKay, Changrim Lee |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Leucine zipper
Biomedical Engineering Pharmaceutical Science 02 engineering and technology Exosome Antibodies Article Antibody fragments Viral Proteins 03 medical and health sciences chemistry.chemical_compound Drug Delivery Systems Albumins Humans Single-chain variable fragment 030304 developmental biology 0303 health sciences biology Proteins 021001 nanoscience & nanotechnology Transmembrane protein Nanostructures chemistry Biochemistry biology.protein Collagen Elastin like polypeptides Heterologous expression Antibody Peptides 0210 nano-technology Single-Chain Antibodies |
| Zdroj: | Adv Drug Deliv Rev |
| ISSN: | 0169-409X |
| DOI: | 10.1016/j.addr.2020.10.017 |
| Popis: | Antibodies possess multiple biologically relevant features that have been engineered into new therapeutic formats. Two examples include the adaptable specificity of their variable (Fv) region and the extension of plasma circulation times through their crystallizable (Fc) region. Since the invention of the single chain variable fragment (scFv) in 1988, antibody variable regions have been re-engineered into a wide variety of multifunctional nanostructures. Among these strategies, peptide-mediated self-assembly of variable regions through heterologous expression has become a powerful method to produce homogenous, functional biomaterials. This manuscript reviews recent reports of antibody fragments assembled through fusion with peptides and proteins, including elastin-like polypeptides (ELPs), collagen-like polypeptides (CLPs), albumin, transmembrane proteins, leucine zippers, silk protein, and viruses. This review further discusses the current clinical status of engineered antibody fragments and challenges to overcome. |
| Databáze: | OpenAIRE |
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