Conjugation of a peptide to an antibody engineered with free cysteines dramatically improves half-life and activity

• Main Authors: Raul C. Camacho (Author), Seohee You (Author), Katharine E. D'Aquino (Author), Wenyu Li (Author), Yuanping Wang (Author), Joseph Gunnet (Author), James Littrell (Author), Jian Shen Qi (Author), Lijuan Kang (Author), Wenying Jian (Author), Mary MacDonald (Author), Timothy Tat (Author), Derek Steiner (Author), Yue-Mei Zhang (Author), James Lanter (Author), Raymond Patch (Author), Rui Zhang (Author), Jiali Li (Author), Suzanne Edavettal (Author), Wilson Edwards (Author), Thai Dinh (Author), Li Ying Wang (Author), Judy Connor (Author), Michael Hunter (Author), Ellen Chi (Author), Ronald V. Swanson (Author), James N. Leonard (Author), Martin A. Case (Author)
• Format: Book
• Published: Taylor & Francis Group, 2020-01-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

The long circulating half-life and inherently bivalent architecture of IgGs provide an ideal vehicle for presenting otherwise short-lived G-protein-coupled receptor agonists in a format that enables avidity-driven enhancement of potency. Here, we describe the site-specific conjugation of a dual agon...