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Peer-reviewedCC BYAdvanced Science

Mechanistic Understanding of Protein–MOF Integration Through Surfactant‐Driven Interfacial Design

  • Ehsan Rashidniyaghi1,2
  • Mohammad Khavani1,2
  • Carlie Coerver1,2
  • Ruibin Liang1,2
  • Raheleh Ravanfar1,2
  1. 1Department of Chemistry and Biochemistry Texas Tech University Lubbock Texas USA
  2. 2Texas Tech University
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Abstract

Integration of proteins into metal-organic frameworks (Protein@MOF) represents an effective method for protein stabilization, with rising demand across material and biomedical sciences. However, the molecular mechanism of protein-MOF interactions remains unsettled due to challenges in developing a general platform to systematically investigate such interactions, hindering improvements in their chemical and physical properties. Here, we develop a surfactant-guided strategy to modulate the assembly of protein@MOF through interfacial design. We discovered that the interfacial environment between proteins and MOFs is the primary factor determining encapsulation efficiency, structural retention, and functional performance. Lipid-based non-ionic surfactants such as glycerol monooleate (GMO) increase the protein's solvent-accessible surface area (SASA), suggesting partial remodeling of the protein surface and hydration shell. GMO at the interface of protein@MOF results in a 20% improvement in protein encapsulation and a 30% increase in MOF growth rate. All-atom molecular dynamics simulations reveal domain-specific interactions between GMO and flexible surface residues on protein in a concentration-dependent manner, involving both electrostatic and hydrophobic contacts. This work offers new molecular insights into how surfactant-driven interfacial design fine-tunes the stability of protein@MOF, laying the foundation for robust alternatives to lipid nanodiscs for membrane protein stabilization, and protein-based platforms for drug-delivery, biocatalysis, and biosensing.

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Cite

BibTeXRIS
BibTeX
@article{rashidniyaghi2026mechanistic,
  title = {{Mechanistic Understanding of Protein–MOF Integration Through Surfactant‐Driven Interfacial Design}},
  author = {Ehsan Rashidniyaghi and Mohammad Khavani and Carlie Coerver and Ruibin Liang and Raheleh Ravanfar},
  journal = {Advanced Science},
  year = {2026},
  month = jun,
  doi = {10.1002/advs.76011},
  url = {https://doi.org/10.1002/advs.76011},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Mechanistic Understanding of Protein–MOF Integration Through Surfactant‐Driven Interfacial Design
AU  - Ehsan Rashidniyaghi
AU  - Mohammad Khavani
AU  - Carlie Coerver
AU  - Ruibin Liang
AU  - Raheleh Ravanfar
PY  - 2026
DA  - 2026/06/09
JO  - Advanced Science
DO  - 10.1002/advs.76011
UR  - https://doi.org/10.1002/advs.76011
AB  - Integration of proteins into metal-organic frameworks (Protein@MOF) represents an effective method for protein stabilization, with rising demand across material and biomedical sciences. However, the molecular mechanism of protein-MOF interactions remains unsettled due to challenges in developing a general platform to systematically investigate such interactions, hindering improvements in their chemical and physical properties. Here, we develop a surfactant-guided strategy to modulate the assembly of protein@MOF through interfacial design. We discovered that the interfacial environment between proteins and MOFs is the primary factor determining encapsulation efficiency, structural retention, and functional performance. Lipid-based non-ionic surfactants such as glycerol monooleate (GMO) increase the protein's solvent-accessible surface area (SASA), suggesting partial remodeling of the protein surface and hydration shell. GMO at the interface of protein@MOF results in a 20% improvement in protein encapsulation and a 30% increase in MOF growth rate. All-atom molecular dynamics simulations reveal domain-specific interactions between GMO and flexible surface residues on protein in a concentration-dependent manner, involving both electrostatic and hydrophobic contacts. This work offers new molecular insights into how surfactant-driven interfacial design fine-tunes the stability of protein@MOF, laying the foundation for robust alternatives to lipid nanodiscs for membrane protein stabilization, and protein-based platforms for drug-delivery, biocatalysis, and biosensing.
SN  - 2198-3844
ER  -