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  1. Article: Hydration behaviors of nonfouling zwitterionic materials.

    Sarker, Pranab / Lu, Tieyi / Liu, Di / Wu, Guangyao / Chen, Hanning / Jahan Sajib, Md Symon / Jiang, Shaoyi / Chen, Zhan / Wei, Tao

    Chemical science

    2023  Volume 14, Issue 27, Page(s) 7500–7511

    Abstract: Zwitterionic materials have emerged as highly effective ultralow fouling materials for many applications, however the underlying mechanism of fouling resistance remains unclear. ... ...

    Abstract Zwitterionic materials have emerged as highly effective ultralow fouling materials for many applications, however the underlying mechanism of fouling resistance remains unclear. Using
    Language English
    Publishing date 2023-06-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d3sc01977b
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Protein Corona on Gold Nanoparticles Studied with Coarse-Grained Simulations.

    Jahan Sajib, Md Symon / Sarker, Pranab / Wei, Yong / Tao, Xiuping / Wei, Tao

    Langmuir : the ACS journal of surfaces and colloids

    2020  Volume 36, Issue 44, Page(s) 13356–13363

    Abstract: Understanding protein corona formation in an aqueous environment at the molecular and atomistic levels is critical to applications such as biomolecule-detection and drug delivery. In this work, we employed mesoscopic coarse-grained simulations to study ... ...

    Abstract Understanding protein corona formation in an aqueous environment at the molecular and atomistic levels is critical to applications such as biomolecule-detection and drug delivery. In this work, we employed mesoscopic coarse-grained simulations to study ovispirin-1 and lysozyme protein coronas on bare gold nanoparticles. Our study showed that protein corona formation is governed by protein-surface and protein-protein interactions, as well as the surface hydrophobic effect. The corona structure was found to be dependent on protein types and the size of nanoparticles. Ovispirin proteins form homogeneous single-layered adsorption in comparison with the lysozyme's inhomogeneous multilayered aggregates on gold NP surfaces. The decrease in nanoparticle size leads to more angular degrees of freedom for protein adsorption orientation. Subsequent atomistic molecular dynamics simulations further demonstrate the loss of secondary structure of ovispirin upon adsorption and the heterogeneity of its local structure.
    MeSH term(s) Adsorption ; Gold ; Metal Nanoparticles ; Nanoparticles ; Protein Corona ; Surface Properties
    Chemical Substances Protein Corona ; Gold (7440-57-5)
    Keywords covid19
    Language English
    Publishing date 2020-10-30
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.0c02767
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Protein Corona on Gold Nanoparticles Studied with Coarse-Grained Simulations

    Jahan Sajib, Md Symon / Sarker, Pranab / Wei, Yong / Tao, Xiuping / Wei, Tao

    Langmuir

    Abstract: Understanding protein corona formation in an aqueous environment at the molecular and atomistic levels is critical to applications such as biomolecule-detection and drug delivery. In this work, we employed mesoscopic coarse-grained simulations to study ... ...

    Abstract Understanding protein corona formation in an aqueous environment at the molecular and atomistic levels is critical to applications such as biomolecule-detection and drug delivery. In this work, we employed mesoscopic coarse-grained simulations to study ovispirin-1 and lysozyme protein coronas on bare gold nanoparticles. Our study showed that protein corona formation is governed by protein-surface and protein-protein interactions, as well as the surface hydrophobic effect. The corona structure was found to be dependent on protein types and the size of nanoparticles. Ovispirin proteins form homogeneous single-layered adsorption in comparison with the lysozyme's inhomogeneous multilayered aggregates on gold NP surfaces. The decrease in nanoparticle size leads to more angular degrees of freedom for protein adsorption orientation. Subsequent atomistic molecular dynamics simulations further demonstrate the loss of secondary structure of ovispirin upon adsorption and the heterogeneity of its local structure.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #899853
    Database COVID19

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  4. Article ; Online: Atomistic Simulations of Biofouling and Molecular Transfer of a Cross-linked Aromatic Polyamide Membrane for Desalination.

    Jahan Sajib, Md Symon / Wei, Ying / Mishra, Ankit / Zhang, Lin / Nomura, Ken-Ichi / Kalia, Rajiv K / Vashishta, Priya / Nakano, Aiichiro / Murad, Sohail / Wei, Tao

    Langmuir : the ACS journal of surfaces and colloids

    2020  Volume 36, Issue 26, Page(s) 7658–7668

    Abstract: Reverse osmosis through a polyamide (PA) membrane is an important technique for water desalination and purification. In this study, molecular dynamics simulations were performed to study the biofouling mechanism (i.e., protein adsorption) and ... ...

    Abstract Reverse osmosis through a polyamide (PA) membrane is an important technique for water desalination and purification. In this study, molecular dynamics simulations were performed to study the biofouling mechanism (i.e., protein adsorption) and nonequilibrium steady-state water transfer of a cross-linked PA membrane. Our results demonstrated that the PA membrane surface's roughness is a key factor of surface's biofouling, as the lysozyme protein adsorbed on the surface's cavity site displays extremely low surface diffusivity, blocking water passage, and decreasing water flux. The adsorbed protein undergoes secondary structural changes, particularly in the pressure-driven flowing conditions, leading to strong protein-surface interactions. Our simulations were able to present water permeation close to the experimental conditions with a pressure difference as low as 5 MPa, while all the electrolytes, which are tightly surrounded by hydration water, were effectively rejected at the membrane surfaces. The analysis of the self-intermediate scattering function demonstrates that the dynamics of water molecules coordinated with hydrogen bonds is faster inside the pores than during the translation across the pores. The pressure difference applied shows a negligible effect on the water structure and content inside the membrane but facilitates the transportation of hydrogen-bonded water molecules through the membrane's sub-nanopores with a reduced coordination number. The linear relationship between the water flux and the pressure difference demonstrates the applicability of continuum hydrodynamic principles and thus the stability of the membrane structure.
    Language English
    Publishing date 2020-06-22
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.0c01308
    Database MEDical Literature Analysis and Retrieval System OnLINE

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