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  • 1.
    Sun, Tianyang
    et al.
    Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK). Zhejiang University, People's Republic of China.
    Han, Guang
    Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
    Lindgren, Matteus
    Shen, Zhijian
    Laaksonen, Aatto
    Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK). Stellenbosch University, South Africa.
    Adhesion of lactoferrin and bone morphogenetic protein-2 to a rutile surface: dependence on the surface hydrophobicity2014In: Biomaterials Science, ISSN 2047-4830, Vol. 2, no 8, p. 1090-1099Article in journal (Refereed)
    Abstract [en]

    Binding of the proteins human lactoferrin (LF) and human bone morphogenetic protein-2 (BMP2) to a hydroxylated TiO2 rutile (110) surface has been modeled using molecular dynamics (MD) simulations. In order to study the effect of the hydrophobicity of the rutile surface on the protein binding process, the rutile surface was made more hydrophilic or more hydrophobic by adjusting the rutile atomic charges. The binding of LF and BMP2 to the hydrophobic rutile surface occurred through direct contact between the protein and rutile via both hydrophobic and hydrophilic amino acids. This forced the proteins to undergo structural rearrangements, observed primarily in BMP2. Binding to the hydrophilic rutile surface was largely indirect via the hydration layer of water on the surface of rutile. Both LF and BMP2 had a higher binding strength to the hydrophobic rutile surfaces than to the hydrophilic surfaces, as seen in the larger amplitude of the binding energies.

  • 2.
    Sun, TianYang
    et al.
    Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK), Physical Chemistry.
    Liang, Li-Jun
    Wang, Qi
    Laaksonen, Aatto
    Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK), Physical Chemistry.
    Wu, Tao
    A molecular dynamics study on pH response of protein adsorbed on peptide-modified polyvinyl alcohol hydrogel2014In: Biomaterials science, ISSN 2047-4830, Vol. 2, no 3, p. 419-426Article in journal (Refereed)
    Abstract [en]

    The interactions between proteins and functional biomaterials under different physical and environmental conditions need to be understood when designing biomedical devices. Herein, we present a molecular dynamics simulation study of the fragment antigen-binding (Fab) of trastuzumab (a monoclonal antibody) and its complex with a peptide-modified polyvinyl alcohol (PVA) hydrogel at different pH values. Consistent with experiments, PVA when modified by charged ligands does shrink as a direct response to a drop in the pH. The protein maintains a stable conformation when adsorbed on the hydrogel matrix with a varied pH, showing no signs of denaturation in all simulated systems, suggesting that peptide-grafted PVA is a good biocompatible material. Under neutral conditions, the hydrogel alone stabilizes the interactions between the protein and the peptide ligands. Strikingly under acidic conditions the protein-ligand interactions are disrupted by a collective protonation of ligands. A sharp decrease in the interaction energies, accompanied by the sudden increase of the protein-ligand distance, indicates a rapid pH response in the protein-hydrogel complex. This will be important in protein delivery and purification. The effect of pH on the interactions and the dynamics of the protein and the sudden pH response of the hydrogel at the atomic level present a new functional perspective in developing new hydrogels with desirable properties.

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