NDLI: Structural influence of proteins upon adsorption to MoS<sub>2</sub> nanomaterials: comparison of MoS<sub>2</sub> force field parameters

Content Provider	Royal Society of Chemistry (RSC)
Author	Gu, Zonglin Yang, Zaixing Luna, Phil De Zhou, Ruhong
Copyright Year	2017
Abstract	Molybdenum disulfide (MoS2) has recently emerged as a promising nanomaterial in a wide range of applications due to its unique and impressive properties. For example, MoS2 has gained attention in the biomedical field because of its ability to act as an antibacterial and anticancer agent. However, the potential influence of this exciting nanomaterial on biomolecules is yet to be extensively studied. Molecular dynamics (MD) simulations are invaluable tools in the examination of protein interactions with nanomaterials such as MoS2. Previous protein MD studies have employed MoS2 force field parameters which were developed to accurately model bulk crystal structures and thermal heat transport but may not necessarily be amendable to its properties at the interface with biomolecules. By adopting a newly developed MoS2 force field, which was designed to better capture its interaction with water and proteins, we have examined the changes in protein structures between the original and refitted MoS2 force field parameters of three representative proteins, polyalanine (α-helix), YAP65 WW-domains (β-sheet), and HP35 (globular protein) when adsorbed onto MoS2 nanomaterials. We find that the original force field, with much larger van der Waals (vdW) contributions, resulted in more dramatic protein structural damage than the refitted parameters. Importantly, some denaturation of the protein tertiary structure and the local secondary structure persisted with the refitted force field albeit overall less severe MoS2 denaturation capacity was found. This work suggests that the denaturation ability of MoS2 to the protein structure is not as dire as previously reported and provides noteworthy findings on the dynamic interactions of proteins with this emergent material.
Starting Page	3039
Ending Page	3045
Page Count	7
File Format	HTM / HTML PDF
ISSN	14639076
Volume Number	19
Issue Number	4
Journal	Physical Chemistry Chemical Physics
DOI	10.1039/c6cp05260f
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Force field (fiction) Molybdenum disulfide Alpha helix Molecular dynamics Nanomaterials Beta sheet Denaturation (biochemistry) Protein structure Biomolecular structure Protein Van der Waals force Globular protein
Content Type	Text
Resource Type	Article
Subject	Physics and Astronomy Physical and Theoretical Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Discrete structure of van der Waals domains in globular proteins (2003)

Adsorption of Methylene Blue on Azo Dye Wastewater by Molybdenum Disulfide Nanomaterials

Two-dimensional MoS2 as a new material for electronic devices

Facile Exfoliation for High-Quality Molybdenum Disulfide Nanoflakes and Relevant Field-Effect Transistors Developed With Thermal Treatment

Temperature Effect of van der Waals Epitaxial GaN Films on Pulse-Laser-Deposited 2D $MoS_{2}$ Layer

Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions

PROTEINS: Structure, Function, and Genetics 25:89-103 (1996) On the Sensitivity of MD Trajectories to Changes in Water-Protein Interaction Parameters: The Potato Carboxypeptidase Inhibitor in Water as a Test Case for

van der Waals trilayers and superlattices: modification of electronic structures of MoS₂ by intercalation

Type-I van der Waals heterostructure formed by MoS₂ and ReS₂ monolayers

Structural influence of proteins upon adsorption to MoS₂ nanomaterials: comparison of MoS₂ force field parameters

Similar Documents

Discrete structure of van der Waals domains in globular proteins (2003)

Adsorption of Methylene Blue on Azo Dye Wastewater by Molybdenum Disulfide Nanomaterials

Two-dimensional MoS2 as a new material for electronic devices

Facile Exfoliation for High-Quality Molybdenum Disulfide Nanoflakes and Relevant Field-Effect Transistors Developed With Thermal Treatment

Temperature Effect of van der Waals Epitaxial GaN Films on Pulse-Laser-Deposited 2D $MoS_{2}$ Layer

Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions

PROTEINS: Structure, Function, and Genetics 25:89-103 (1996) On the Sensitivity of MD Trajectories to Changes in Water-Protein Interaction Parameters: The Potato Carboxypeptidase Inhibitor in Water as a Test Case for

van der Waals trilayers and superlattices: modification of electronic structures of MoS2 by intercalation

Type-I van der Waals heterostructure formed by MoS2 and ReS2 monolayers

Structural influence of proteins upon adsorption to MoS2 nanomaterials: comparison of MoS2 force field parameters

van der Waals trilayers and superlattices: modification of electronic structures of MoS₂ by intercalation

Type-I van der Waals heterostructure formed by MoS₂ and ReS₂ monolayers

Structural influence of proteins upon adsorption to MoS₂ nanomaterials: comparison of MoS₂ force field parameters