Mechanical and biological deterioration of articular cartilage is an irreversible process retarded by lubricin (PRG4) —a mucinous glycoprotein that naturally forms a protective coating on the cartilage surface. Drawing inspiration from lubricin’s structure, we designed a new set of bioconjugates with protein-based binding domains and antifouling brush polymers. We synthesizedf these bioconjugates by combining ATRP and copper-catalyzed click chemistry, and characterized them by NMR, IR, GPC, SLS, and SDS-PAGE. Our click-based modular synthesis approach allows for compatibility with a large variety of proteins and functional polymers. Furthermore, we studied the adsorption behavior of our brush copolymers onto collagen by quartz crystal microbalance (QCM) and, investgated their conformatinal mechanics by colloidal probe atomic force microscopy (CP-AFM). We will discuss our findings in the context of our previous work on the conformational mechanics of PRG4. Our results contribute to the rational design of innovative, bio-inspired, polymers for the treatment of osteoarthritis.