Site-Specific Antibody Conjugation Using Modified Bisected -Glycans: Method Development and Potential toward Tunable Effector Function.

Antibody-drug conjugates (ADCs) have garnered worldwide attention for disease treatment, as they possess high target specificity, a long half-life, and outstanding potency to kill or modulate the functions of targets. FDA approval of multiple ADCs for cancer therapy has generated a strong desire for novel conjugation strategies with high biocompatibility and controllable bioproperties. Herein, we present a bisecting glycan-bridged conjugation strategy that enables site-specific conjugation without the need for the oligosaccharide synthesis and genetic engineering of antibodies.

Scalable synthesis of the unusual amino acid segment (ADMOA unit) of marine anti-inflammatory peptide: solomonamide A.

The most abundantly available hexose sugar, d-glucose has been converted to protected 4-amino(2'amino-4'-hydroxy phenyl)-3,5-dihydroxy-2-methyl-6-oxo hexanoic acid (protected ADMOA, 3), the unusual amino acid present in marine natural product solomonamide A in gram quantities involving easy to operate chemical transformations.