Oriented immobilization of proteins on hydroxyapatite surface using bifunctional bisphosphonates as linkers

Biomacromolecules
Jivan N YewleLeonidas G Bachas

Abstract

Oriented immobilization of proteins is an important step in creating protein-based functional materials. In this study, a method was developed to orient proteins on hydroxyapatite (HA) surfaces, a widely used bone implant material, to improve protein bioactivity by employing enhanced green fluorescent protein (EGFP) and β-lactamase as model proteins. These proteins have a serine or threonine at their N-terminus that was oxidized with periodate to obtain a single aldehyde group at the same location, which can be used for the site-specific immobilization of the protein. The HA surface was modified with bifunctional hydrazine bisphosphonates (HBPs) of various length and lipophilicity. The number of functional groups on the HBP-modified HA surface, determined by a 2,4,6-trinitrobenzenesulfonic acid (TNBS) assay, was found to be 2.8 × 10(-5) mol/mg of HA and unaffected by the length of HBPs. The oxidized proteins were immobilized on the HBP-modified HA surface in an oriented manner through formation of a hydrazone bond. The relative protein immobilization amounts through various HBPs were determined by fluorescence and bicinchoninic acid (BCA) assay and showed no significant effect by length and lipophilicity of HBPs. The relative a...Continue Reading

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Aug 6, 2014·Colloids and Surfaces. B, Biointerfaces·Wing-Hin LeeRamin Rohanizadeh
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Feb 12, 2020·International Journal of Biological Macromolecules·Thamara C CoutinhoCristiane S Farinas
Aug 30, 2021·Biotechnology Advances·Rafael C RodriguesRoberto Fernandez-Lafuente

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