Tailoring Fusion Proteins for Interfacial Nanoparticle Functionalization: Toward Fluorescence-Guided Imaging
4 affiliations
- 1Federal University of Paraná , , , ,
- 2Federal Technological University of Paraná , , , ,
- 3Brazilian Center for Research in Energy and Materials , , , ,
- 4Araguaia University Center , , ,
Abstract
Fusion proteins are specially designed molecules created by linking two or more peptides that were originally encoded by separate DNA sequences. To improve control of protein adsorption on poly(3-hydroxybutyrate) (PHB) surfaces, we developed fusion proteins comprising a polyester substrate-binding domain (SBD) fused to superfolder green fluorescent protein (sfGFP). The subunits were connected via flexible (GGGGS)n or rigid (EAAAK)n linkers with n = 1, 2, or 4. The PHB immobilization efficiency provided by these fusion proteins was extensively evaluated on microparticles and nanoparticles by using various surface-sensitive techniques. Accordingly, constructs linked by rigid sequences with n = 2 and n = 4 exhibited higher PHB adsorption capability. This suggests that reduced interdomain conformational freedom may favor configurations compatible with SBD-mediated interaction with the PHB interface. The stable association of the constructs with PHB nanoparticles enabled fluorescence-based tracking during cellular uptake experiments. The spatial orientation and polyester-binding ability conferred by such constructs via a facile, mild, and persistent association process might represent a significant biotechnological advance in the development of advanced nanosystems sensitive to fluorescence imaging.
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BibTeX
@article{masaki2026tailoring,
title = {{Tailoring Fusion Proteins for Interfacial Nanoparticle Functionalization: Toward Fluorescence-Guided Imaging}},
author = {Ryu Masaki and Julia T. Lucena and Maritza A. Todo Bom and Isabela P. Dias and Mariana Vodiani and Giovanna Furman and Joslaine Jacumazo and Rilton A. de Freitas and Guinther Kellerman and Maísa Colodel and Luiz M. de L. Faria and Gabriela C. Cardoso and Edneia A. S. Ramos and Lindomar J. C. Albuquerque and Genilza da Silva Mello and Camila de Almeida Salvego and Breno C. B. Beirão and Edileusa M. Gerhardt and Emanuel Maltempi de Souza and Marcelo Müller-Santos and Guilherme F. Picheth},
journal = {ACS Omega},
year = {2026},
month = oct,
doi = {10.1021/acsomega.6c09485},
url = {https://pubs.acs.org/acsodf/article/11/42/65865/5450557/Tailoring-Fusion-Proteins-for-Interfacial},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Tailoring Fusion Proteins for Interfacial Nanoparticle Functionalization: Toward Fluorescence-Guided Imaging
AU - Ryu Masaki
AU - Julia T. Lucena
AU - Maritza A. Todo Bom
AU - Isabela P. Dias
AU - Mariana Vodiani
AU - Giovanna Furman
AU - Joslaine Jacumazo
AU - Rilton A. de Freitas
AU - Guinther Kellerman
AU - Maísa Colodel
AU - Luiz M. de L. Faria
AU - Gabriela C. Cardoso
AU - Edneia A. S. Ramos
AU - Lindomar J. C. Albuquerque
AU - Genilza da Silva Mello
AU - Camila de Almeida Salvego
AU - Breno C. B. Beirão
AU - Edileusa M. Gerhardt
AU - Emanuel Maltempi de Souza
AU - Marcelo Müller-Santos
AU - Guilherme F. Picheth
PY - 2026
DA - 2026/10/13
JO - ACS Omega
DO - 10.1021/acsomega.6c09485
UR - https://pubs.acs.org/acsodf/article/11/42/65865/5450557/Tailoring-Fusion-Proteins-for-Interfacial
AB - Fusion proteins are specially designed molecules created by linking two or more peptides that were originally encoded by separate DNA sequences. To improve control of protein adsorption on poly(3-hydroxybutyrate) (PHB) surfaces, we developed fusion proteins comprising a polyester substrate-binding domain (SBD) fused to superfolder green fluorescent protein (sfGFP). The subunits were connected via flexible (GGGGS)n or rigid (EAAAK)n linkers with n = 1, 2, or 4. The PHB immobilization efficiency provided by these fusion proteins was extensively evaluated on microparticles and nanoparticles by using various surface-sensitive techniques. Accordingly, constructs linked by rigid sequences with n = 2 and n = 4 exhibited higher PHB adsorption capability. This suggests that reduced interdomain conformational freedom may favor configurations compatible with SBD-mediated interaction with the PHB interface. The stable association of the constructs with PHB nanoparticles enabled fluorescence-based tracking during cellular uptake experiments. The spatial orientation and polyester-binding ability conferred by such constructs via a facile, mild, and persistent association process might represent a significant biotechnological advance in the development of advanced nanosystems sensitive to fluorescence imaging.
SN - 2470-1343
ER -