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Destabilization of amyloid fibrils on interaction with MoS2-based nanomaterials
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Theoretical Chemistry and Biology.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Theoretical Chemistry and Biology.ORCID iD: 0000-0003-0185-5724
Cent Leather Res Inst, CSIR, Chem Lab, Chennai 600020, India..
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Theoretical Chemistry and Biology. Henan Univ, Coll Chem & Chem Engn, Kaifeng 475004, Henan, Peoples R China..ORCID iD: 0000-0002-1763-9383
2019 (English)In: RSC Advances, ISSN 2046-2069, E-ISSN 2046-2069, Vol. 9, no 3, p. 1613-1624Article in journal (Refereed) Published
Abstract [en]

The present work is motivated by the established concept that the structure and energetics of biomacromolecules can be modulated by confining their dimensions in the nanoscale. In particular, here we use force-field methods to understand the stability of amyloid fibrils at nanostructured interfaces, which can be useful for the development of new therapeutics for Alzheimer's disease. We explore the binding modes and structural properties of fibrils at the interface of molybdenum disulphide nanotubes and the nanosurface using classical molecular dynamics simulations. We find that in general the MoS2 materials induces disruptions in the structure of the amyloid fibrils where the beta sheet conformation of the fibrils changes to a turned conformation, and it is large in the case of nanotubes in comparison to the nanosurfaces. The intermolecular hydrogen bonds, hydrophilic and hydrophobic contacts between the monomer peptides in the fibril are reduced due to their adsorption onto the MoS2 materials, which results in a destabilization of the fibril. The destabilization of fibril is to some extent compensated for by the van der Waals interactions between the fibril and MoS2. Overall the results indicate that MoS2-based materials can be useful in inhibiting the aggregation of smaller protofibrils to matured fibrils and to bust the already formed fibrils. Therapeutic materials should not exhibit any cross interaction with other off-targets compounds. In order to test whether the MoS2 nanomaterial has any such effect we have studied its interaction with two additional biomacromolecules, the human serum albumin and p53 protein, and we report no significant changes in the secondary structure of these biomolecules. Through molecular docking studies we also established that the drug binding ability of HSA is not altered by its surface binding to MoS2 nanosurface.

Place, publisher, year, edition, pages
ROYAL SOC CHEMISTRY , 2019. Vol. 9, no 3, p. 1613-1624
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-244120DOI: 10.1039/c8ra10184aISI: 000457292800050Scopus ID: 2-s2.0-85060139369OAI: oai:DiVA.org:kth-244120DiVA, id: diva2:1289743
Note

QC 20190219

Available from: 2019-02-19 Created: 2019-02-19 Last updated: 2019-02-19Bibliographically approved

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Mudedla, Sathish KumarNatarajan Arul, MuruganÅgren, Hans

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