Abstract
Real staying power: A subset of bovine antibodies (blue, see scheme) feature an ultralong CDR3 loop that forms an antiparallel β-sheet stalk, terminating in a folded, disulfide cross-linked knob domain. Fusion of a polypeptide (red) into this unique CDR3 motif provides a novel strategy for generating polypeptide therapeutics with enhanced pharmacokinetics and pharmacodynamics. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.