Proteinized Surface Remodeling Decouples Environmental Stability from Intracellular Degradation in Oxidation-Prone 2D Nanoborophene.
10 affiliations
- 1Department of Nuclear Engineering, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
- 2Huck Institutes of the Life Sciences, 101 Huck Life Sciences Building, University Park, Pennsylvania16802, United States.
- 3Department of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
- 4Department of Bioengineering, Institute of Natural Sciences, Ege University, Izmir35100, Türkiye.
- 5Department of Materials Science and Engineering, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
- 6Surface Analysis Facility, University of Delaware, Newark, Delaware19716, United States.
- 7Tomocube Inc., San Diego, California92108, United States.
- 8Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
- 9Materials Research Institute, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
- 10Center for Infectious Disease Dynamics, The Pennsylvania State University, University Park, Pennsylvania16802, United States.
Abstract
Borophene (BPH), a monolayer boron allotrope, exhibits outstanding electrical and mechanical properties but remains intrinsically constrained by its excessive susceptibility to oxidative degradation in aqueous and physiological environments. This study demonstrates that protein-assisted exfoliation using human serum albumin (HSA) establishes a dynamic biointerfacial sheath (BIS) that decouples environmental stability from intracellular degradation. HSA forms a robust BIS via multivalent hydrophobic, electrostatic, and thiol-mediated interactions, driving exfoliation into ultrathin nanosheets while suppressing air- and serum-induced oxidation. Proteinized BPH (PBPH) shows enhanced extracellular colloidal and chemical stability; however, upon cellular uptake, the same interface promotes rapid reactive oxygen species-driven degradation, leading to lattice fragmentation, loss of crystallinity, and conversion into soluble boronate species. Multimodal analyses confirm accelerated degradation kinetics and environmental stability of PBPH. These results highlight the protein corona as an active regulator of nanomaterial fate, enabling programmable decoupling of extracellular persistence from intracellular clearance in oxidation-prone two-dimensional systems.
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BibTeX
@article{saha2026proteinized,
title = {{Proteinized Surface Remodeling Decouples Environmental Stability from Intracellular Degradation in Oxidation-Prone 2D Nanoborophene.}},
author = {Pranay Saha and Shraddha Krishnakumar and Teresa Aditya and Nada Maher and Aysenur Yardim and Oguzhan Colak and David Skrodzki and Sung Hyun Cho and Xu Feng and Dongjun Shin and Dipanjan Pan},
journal = {ACS nano},
year = {2026},
month = sep,
doi = {10.1021/acsnano.6c11186},
url = {https://europepmc.org/article/MED/42916092},
note = {CC BY},
}
RIS
TY - JOUR
TI - Proteinized Surface Remodeling Decouples Environmental Stability from Intracellular Degradation in Oxidation-Prone 2D Nanoborophene.
AU - Pranay Saha
AU - Shraddha Krishnakumar
AU - Teresa Aditya
AU - Nada Maher
AU - Aysenur Yardim
AU - Oguzhan Colak
AU - David Skrodzki
AU - Sung Hyun Cho
AU - Xu Feng
AU - Dongjun Shin
AU - Dipanjan Pan
PY - 2026
DA - 2026/09/01
JO - ACS nano
DO - 10.1021/acsnano.6c11186
UR - https://europepmc.org/article/MED/42916092
AB - Borophene (BPH), a monolayer boron allotrope, exhibits outstanding electrical and mechanical properties but remains intrinsically constrained by its excessive susceptibility to oxidative degradation in aqueous and physiological environments. This study demonstrates that protein-assisted exfoliation using human serum albumin (HSA) establishes a dynamic biointerfacial sheath (BIS) that decouples environmental stability from intracellular degradation. HSA forms a robust BIS via multivalent hydrophobic, electrostatic, and thiol-mediated interactions, driving exfoliation into ultrathin nanosheets while suppressing air- and serum-induced oxidation. Proteinized BPH (PBPH) shows enhanced extracellular colloidal and chemical stability; however, upon cellular uptake, the same interface promotes rapid reactive oxygen species-driven degradation, leading to lattice fragmentation, loss of crystallinity, and conversion into soluble boronate species. Multimodal analyses confirm accelerated degradation kinetics and environmental stability of PBPH. These results highlight the protein corona as an active regulator of nanomaterial fate, enabling programmable decoupling of extracellular persistence from intracellular clearance in oxidation-prone two-dimensional systems.
SN - 1936-0851
SN - 1936-086X
ER -