Molecular Dynamics Simulation on Stability of Insulin on Graphene

Liang, Lijun; Wang, Qi; Wu, Tao; Shen, Jia-Wei; Kang, Yu

doi:10.1088/1674-0068/22/06/627-634

Cited by 26 publications

(18 citation statements)

References 36 publications

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“…High contact stabilities were found for both the aromatic tyrosine (Tyr63) and phenylalanine (Phe67) residues with all nanomaterials. The stable π-stacking arrangements between the aromatic rings of the peptide and the electron-rich carbon rings of the surface, suggest that these are the key residues that contribute to the strong interactions between the peptide and the carbonaceous nanomaterials, in line with other studies [23] , [30] – [32] , [52] , [77] , [78] .…”

Section: Resultssupporting

confidence: 86%

“…This feature was determined as fibril-favoring in our previous works on apoC-II(60-70) oligomers [34] , [37] . Other studies have also shown that carbon nanotubes and graphene surfaces facilitate a change in the conformation of peptides [30] , [77] and π-stacking is an efficient mode of biological recognition of π-electron-rich carbon nanoparticles [23] , [30] – [32] , [52] , [77] , [78] .…”

Section: Resultsmentioning

confidence: 97%

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Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations

Todorova¹,

Makarucha²,

Hine

et al. 2013

PLoS Comput Biol

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Experimental studies have demonstrated that nanoparticles can affect the rate of protein self-assembly, possibly interfering with the development of protein misfolding diseases such as Alzheimer's, Parkinson's and prion disease caused by aggregation and fibril formation of amyloid-prone proteins. We employ classical molecular dynamics simulations and large-scale density functional theory calculations to investigate the effects of nanomaterials on the structure, dynamics and binding of an amyloidogenic peptide apoC-II(60-70). We show that the binding affinity of this peptide to carbonaceous nanomaterials such as C60, nanotubes and graphene decreases with increasing nanoparticle curvature. Strong binding is facilitated by the large contact area available for π-stacking between the aromatic residues of the peptide and the extended surfaces of graphene and the nanotube. The highly curved fullerene surface exhibits reduced efficiency for π-stacking but promotes increased peptide dynamics. We postulate that the increase in conformational dynamics of the amyloid peptide can be unfavorable for the formation of fibril competent structures. In contrast, extended fibril forming peptide conformations are promoted by the nanotube and graphene surfaces which can provide a template for fibril-growth.

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Section: Resultssupporting

confidence: 86%

Section: Resultsmentioning

confidence: 97%

Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations

Todorova¹,

Makarucha²,

Hine

et al. 2013

PLoS Comput Biol

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“…Molecular dynamics simulation predicted that human insulin can be adsorbed onto graphene surfaces and that some proteins would be destroyed or partially destroyed. 142 Water-soluble graphene oxide nanosheets (GO) are oxidation products of graphene nanosheets. GOs have a stronger serum protein adsorption capability than SWNT or MWNT.…”

Section: Nanoparticle-biomolecule Interactionsmentioning

confidence: 99%

Chemical Basis of Interactions Between Engineered Nanoparticles and Biological Systems

et al. 2014

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“…GBM-hormone interactions. In addition to serum proteins, graphene substrates have also shown strong propensity to interact with hormones present in serum 36,37 . A molecular simulation study demonstrated how insulin hormones present in serum can interact with graphene ribbon-like surfaces of different sizes 36 .…”

Section: Gbm-biomolecular Interactionsmentioning

confidence: 99%

Linking graphene-based material physicochemical properties with molecular adsorption, structure and cell fate

Kumar

Parekh

2020

Commun Chem

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Graphene, an allotrope of carbon, consists of a single layer of carbon atoms with uniquely tuneable properties. As such, graphene-based materials (GBMs) have gained interest for tissue engineering applications. GBMs are often discussed in the context of how different physicochemical properties affect cell physiology, without explicitly considering the impact of adsorbed proteins. Establishing a relationship between graphene properties, adsorbed proteins, and cell response is necessary as these proteins provide the surface upon which cells attach and grow. This review highlights the molecular adsorption of proteins on different GBMs, protein structural changes, and the connection to cellular function.O ver the past decade, graphene and graphene-based materials (GBMs), such as graphene oxide (GO), reduced graphene oxide (RGO), and their chemical derivatives, have gained substantial interest for the development of biomaterials for tissue engineering applications. The unique physicochemical properties of graphene and GBMs have been shown to significantly influence cell response, as previously reviewed 1,2 . In our previous review article, we highlighted the influence of GBM physical (roughness, topography, conductivity, and lateral dimension), chemical (wettability, surface functional moieties, and chemical interaction), and mechanical properties on cell response, without explicitly discussing how GBMs influence protein or biomolecular interaction 3 . The effect of graphene physicochemistry on biomolecular interactions of proteins has been reviewed separately 4-6 . Since proteins on biomaterial surfaces are a key mediator of subsequent cell behavior for nanomaterials 7-9 , the unique physicochemical properties of graphene offer exciting opportunities to control protein adsorption, orientation, conformation, and ultimately cell fate.The adsorbed protein distribution and conformation on biomaterial surfaces provide the cellinterfacing topographical, physical, and biochemical cues for cells to interact with and respond to a material 10 . Studies have demonstrated that a material's ability to adsorb proteins (e.g., albumin, vitronectin (Vn), fibronectin (Fn), collagen, and laminin) from the serum of cell culture media plays a vital role in cellular attachment and function 8,11 . Moreover, adsorption of the same protein but with different conformations, which exposes different domains to cells, has been

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Molecular Dynamics Simulation on Stability of Insulin on Graphene

Cited by 26 publications

References 36 publications

Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations

Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations

Chemical Basis of Interactions Between Engineered Nanoparticles and Biological Systems

Linking graphene-based material physicochemical properties with molecular adsorption, structure and cell fate

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