Journal
PROTEIN ENGINEERING DESIGN & SELECTION
Volume 27, Issue 10, Pages 325-330Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzu043
Keywords
fusion proteins; hydrodynamic radius; linker design; size-exclusion chromatography
Funding
- Bill and Melinda Gates Foundation through Grand Challenges in Global Health Initiative
- Director's Pioneer Award [1DP1OD006961-01]
- National Institutes of Health HIVRAD [P01A1100148]
- NIDA/National Institutes of Health
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Engineered fusion proteins containing two or more functional polypeptides joined by a peptide or protein linker are important for many fields of biological research. The separation distance between functional units can impact epitope access and the ability to bind with avidity; thus the availability of a variety of linkers with different lengths and degrees of rigidity would be valuable for protein design efforts. Here, we report a series of designed structured protein linkers incorporating naturally occurring protein domains and compare their properties to commonly used Gly(4)Ser repeat linkers. When incorporated into the hinge region of an immunoglobulin G (IgG) molecule, flexible Gly(4)Ser repeats did not result in detectable extensions of the IgG antigen-binding domains, in contrast to linkers including more rigid domains such as beta 2-microglobulin, Zn-alpha 2-glycoprotein and tetratricopeptide repeats. This study adds an additional set of linkers with varying lengths and rigidities to the available linker repertoire, which may be useful for the construction of antibodies with enhanced binding properties or other fusion proteins.
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