The proximity of the N- and C- termini of bovine knob domains enable engineering of target specificity into polypeptide chains

The proximity of the N- and C- termini of bovine knob domains enable engineering of target specificity into polypeptide chains

Cysteine-rich knob domains can be isolated from the ultralong heavy-chain complementarity-determining region (CDR) 3, which are unique to a subset of bovine antibodies, to create antibody fragments of ~4 kDa. Advantageously, the N- and C- termini of these small binding domains are in close proximity...

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Bibliographic Details
Main Authors: Alice Hawkins, Callum Joyce, Kevin Brady, Adam Hold, Alan Smith, Michael Knight, Conor Howard, Jean van den Elsen, Alastair D.G. Lawson, Alex Macpherson
Format: Article
Language:English
Published: Taylor & Francis Group 2022-12-01
Series:mAbs
Subjects:
Bovine antibodies
complement C5
knob domain
serum albumin
bispecific
VHH
Online Access:https://www.tandfonline.com/doi/10.1080/19420862.2022.2076295

Internet

https://www.tandfonline.com/doi/10.1080/19420862.2022.2076295

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