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Updated: Aug 13, 2026

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
Published on: August 26, 2013
Bone morphogenetic protein-2 binds as multilayers to a collagen delivery matrix: an equilibrium thermodynamic
Randy Morin1, David Kaplan, Bernardo Perez-Ramirez
1Formulation and Process Development, Wyeth BioPharma, One Burt Road, Andover, MA 01810, USA.
Abstract:
Recombinant human bone morphogenetic protein-2 (rhBMP-2) promotes bone growth but must be retained at the delivery site for optimal efficacy in vivo. rhBMP-2 release from a collagen-based matrix has shown favorable pharmacokinetics. The present study assessed binding affinity and binding saturation of rhBMP-2 to a collagen matrix as a function of solution and rhBMP-2 isoform variables. Results indicate that rhBMP-2 binds to the collagen matrix with affinities on the order of 10(3) to 10(4) M(-1). Maximum binding, nu, was primarily a function of pH for heterogeneous rhBMP-2 and the extended (T(266)/T(266)) isoform. However, binding saturation of the
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