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Molecular dynamics simulation studies of the structural response of an isolated Aβ1–42 monomer localized in the vicinity of the hydrophilic TiO2 surface

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Abstract

We have probed the effect of a model hydrophilic surface, rutile TiO2, on the full-length amyloid beta (Aβ1–42) monomer using molecular dynamics simulations. The rutile surface brings about sharp changes in the peptide’s intrinsic behavior in a distance-dependent manner. The intrinsic collapse of the peptide is disrupted, while the β-sheet propensity is sharply enhanced with increased proximity to the surface. The results may have implications for Aβ self-assembly and fibrillogenesis on hydrophilic surfaces and should be taken into consideration in the design of novel nanomaterials for perturbing amyloidogenic behavior.

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Acknowledgments

J.C.J. thanks the Council of Scientific and Industrial Research for her current Senior Research fellowship. The authors are grateful for financial assistance provided through the Multi-Scale Simulation and Modeling project (MSM), CSIR. CSIR-NCL, Pune, is acknowledged for startup funds and facilities provided through the Centre of Excellence in Scientific Computing. Financial assistance received from the Center of Excellence in Polymers (CoEP-SPIRIT), established from funding received from the Department of Chemicals and Petrochemicals is also acknowledged. J.C.J. would like to thank Mr. Mudit Dixit for help in generating the TiO2 surface.

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  1. Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune, 411008, India

    Jaya C. Jose & Neelanjana Sengupta

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  1. Jaya C. Jose
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Correspondence to Neelanjana Sengupta.

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249_2013_900_MOESM1_ESM.doc

Supplementary material 1 (supplementary material associated with this article consists of plots depicting residue-wise β-sheet fractions; residue-wise alpha helix fractions; histogram of internal non-bonded energies of the peptide in systems A, B, C, and F; histogram of the distance between salt bridge-forming atoms in E22-K28 and D23-K28 for system A, B, and C; histogram of electrostatic interaction energy of the side chains of E22-K28 and D23-K28 with the TiO2 surface for systems A, B, and C.)

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Jose, J.C., Sengupta, N. Molecular dynamics simulation studies of the structural response of an isolated Aβ1–42 monomer localized in the vicinity of the hydrophilic TiO2 surface. Eur Biophys J 42, 487–494 (2013). https://doi.org/10.1007/s00249-013-0900-6

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