1 research outputs found
Rationally Tailored Mesoporous Hosts for Optimal Protein Encapsulation
Proteins play important roles in the therapeutic, medical
diagnostic,
and chemical catalysis industries. However, their potential is often
limited by their fragile and dynamic nature outside cellular environments.
The encapsulation of proteins in solid materials has been widely pursued
as a route to enhance their stability and ease of handling. Nevertheless,
the experimental investigation of protein interactions with rationally
designed synthetic hosts still represents an area in need of improvement.
In this work, we leveraged the tunability and crystallinity of metal–organic
frameworks (MOFs) and developed a series of crystallographically defined
protein hosts with varying chemical properties. Through systematic
studies, we identified the dominating mechanisms for protein encapsulation
and developed a host material with well-tailored properties to effectively
encapsulate the protein ubiquitin. Specifically, in our mesoporous
hosts, we found that ubiquitin encapsulation is thermodynamically
favored. A more hydrophilic encapsulation environment with favorable
electrostatic interactions induces enthalpically favored ubiquitin–MOF
interactions, and a higher pH condition reduces the intraparticle
diffusion barrier, both leading to a higher protein loading. Our findings
provide a fundamental understanding of host–guest interactions
between proteins and solid matrices and offer new insights to guide
the design of future protein host materials to achieve optimal protein
loading. The MOF modification technique used in this work also demonstrates
a facile method to develop materials easily customizable for encapsulating
proteins with different surface properties