# Controlling Protein Immobilization over Poly(3-hydroxybutyrate) Microparticles Using Substrate Binding Domain from PHA Depolymerase

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- Authors: Isabela P. Dias, Regiane Stafim Cunha, Ryu Masaki, Maritza A. Todo Bom, Edneia A. S. Ramos, Giovanna J. V. P. Santos, Giovanna Furman, Julia T. Lucena, Isabella G. Jiacomini, Sze M. Lo, Zelinda Schemczssen-Graeff, Breno C. B. Beirão, Silvio M. Zanata, Luiz M. de L. Faria, Edileusa M. Gerhardt, Emanuel Maltempi Souza, Marcelo Müller-Santos, Guilherme F. Picheth
- Journal: Biomacromolecules
- Year: 2025
- Volume: 26
- Pages: 2529-2539
- DOI: 10.1021/acs.biomac.5c00010
- Instrument used: openQCM 1

## Abstract

Biointerface decoration with ligands is a crucial requirement to modulate biodistribution, increase half-life, and provide navigation control for targeted micro- or nanostructured systems. To better control the process of ligand functionalization over three-dimensional (3D) polyester surfaces, we report the characterization of hybrid proteins developed to enhance the anchoring efficiency over polymeric surfaces and preserve optimal spatial orientation: sfGFP, mRFP1, and the RBD proteins were attached to a polyester substrate binding domain (SBD) formed by the C-terminus region of PHA depolymerase. The binding ability was evaluated over poly(3-hydroxybutyrate) (PHB) microparticles (MP) and two-dimensional (2D) surfaces. The PHB interfaces revealed a high affinity toward the proteins linked with SBD, displaying higher protein contents compared to untagged proteins. The MP decorated with RBD-SBD exhibited limited MRC5 internalization and cytotoxicity without a significant impact caused by the RBD protein, suggesting that the system might be adapted for targeted drug delivery and vaccine applications.

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