Interaction of collagen like peptides with gold nanosurfaces: a molecular dynamics investigation

Gopalakrishnan, R; Singam, Ettayapuram Ramaprasad Azhagiya; Sundar, J. Vijaya; Subramanian, V.

doi:10.1039/c4cp04969a

Cited by 28 publications

(27 citation statements)

References 59 publications

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“…[4][5][6][7] Metallic nanoparticles such as AuNPs might be used in gel form 8 or incorporated into scaffolds 9 to treat wounds as a novel strategy. The unique properties of AuNPs involve enhanced mechanical stability and resistance against enzymatic degradation when incorporated into tissue scaffolds, 10,11 easy incorporation of antibodies, 12 growth factors, 13 and peptides 14 at the surface of AuNPs, enhanced biocompatibility, 15,16 anti-inflammatory, 17 and antimicrobial properties. [18][19][20] These characteristics of AuNPs make them promising candidates for skin tissue engineering applications.…”

Section: Introductionmentioning

confidence: 99%

Collagen/gold nanoparticle nanocomposites: A potential skin wound healing biomaterial

et al. 2016

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In this study, nanocomposite collagen scaffolds incorporating gold nanoparticles (AuNPs) were prepared for wound healing applications. Initially, dose (<20 ppm) and size (>20 nm) of AuNPs that were not cytotoxic on HaCat keratinocytes and 3T3 fibroblasts were determined. Both collagen sponges and AuNP-incorporated nanocomposites (CS-Au) were cross-linked with glutaraldehyde (CS-X and CS-AuX). Incorporation of AuNPs into cross-linked scaffolds enhanced their stability against enzymatic degradation and increased the tensile strength. Hydrolytic degradation of CS-Au group was also less than CS after seven days. Upon confirming in vitro biocompatibility of the scaffolds with cytotoxicity assays, cell attachment and proliferation tests and the in vivo efficacy for healing of full-thickness skin wounds were investigated by applying CS-X, CS-AuX or a commercial product (Matriderm®) onto defect sites and covering with Ioban® drapes. Defects were covered only with drapes for untreated control group. The wound areas were examined with histopathological and biomechanical tests after 14 days of operation. CS-AuX group was superior to untreated control and Matriderm®; it suppressed the inflammation while significantly promoting granulation tissue formation. Inflammatory reaction against CS-AuX was milder than CS-X. Neovascularization was also higher in CS-AuX than other groups, though the result was not significant. Wound closure in CS-X (76%), CS-AuX (69%), and Matriderm® (65%) were better than untreated control (45%). CS-AuX group had the highest tensile strength (significantly higher than Matriderm®) and modulus (significantly higher than Matriderm® and CS-X), indicating a faster course of dermal healing. Further studies are also needed to investigate whether higher loading of AuNPs affects these results positively in a statistically meaningful manner. Overall, their contribution to the enhancement of degradation profiles and mechanical properties, their excellent in vitro biocompatibility, and tendency to accelerate wound healing are encouraging the use of AuNPs in collagen sponges as potent skin substitutes in the future.

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Section: Introductionmentioning

confidence: 99%

Collagen/gold nanoparticle nanocomposites: A potential skin wound healing biomaterial

et al. 2016

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“…The dashed line at Ϫ4.5 ppb/°C is the cutoff for hydrogen-bond formation. Chemical shift changes more positive than Ϫ4.5 ppb/°C are indicative of stable hydrogen bonds(73). C, { 1 H}-15 N heteronuclear NOEs, measured at 15°C, of T3-237 WT, T3-237 G240A, and T3-237 G240V.…”

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confidence: 99%

Molecular underpinnings of integrin binding to collagen-mimetic peptides containing vascular Ehlers–Danlos syndrome–associated substitutions

Hoop

Kemraj

Wang

et al. 2019

Journal of Biological Chemistry

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Collagens carry out critical extracellular matrix (ECM) functions by interacting with numerous cell receptors and ECM components. Single glycine substitutions in collagen III, which predominates in vascular walls, result in vascular Ehlers-Danlos syndrome (vEDS), leading to arterial, uterine, and intestinal rupture and an average life expectancy of <50 years. Collagen interactions with integrin ␣ 2 ␤ 1 are vital for platelet adhesion and activation; however, how these interactions are impacted by vEDS-associated mutations and by specific amino acid substitutions is unclear. Here, we designed collagen-mimetic peptides (CMPs) with previously reported Gly 3 Xaa (Xaa ‫؍‬ Ala, Arg, or Val) vEDS substitutions within a high-affinity integrin ␣ 2 ␤ 1binding motif, GROGER. We used these peptides to investigate, at atomic-level resolution, how these amino acid substitutions affect the collagen III-integrin ␣ 2 ␤ 1 interaction. Using a multitiered approach combining biological adhesion assays, CD, NMR, and molecular dynamics (MD) simulations, we found that these substitutions differentially impede human mesenchymal stem cell spreading and integrin ␣ 2-inserted (␣ 2 I) domain binding to the CMPs and were associated with triple-helix destabilization. Although an Ala substitution locally destabilized hydrogen bonding and enhanced mobility, it did not significantly reduce the CMP-integrin interactions. MD simulations suggested that bulkier Gly 3 Xaa substitutions differentially disrupt the CMP-␣ 2 I interaction. The Gly 3 Arg substitution destabilized CMP-␣ 2 I side-chain interactions, and the Gly 3 Val change broke the essential Mg 2؉ coordination. The relationship between the loss of functional binding and the type of vEDS substitution provides a foundation for developing potential therapies for managing collagen disorders.

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“…Interestingly, these values are agreement with those obtained in earlier simulation work on proteins adsorbed on SAMs 32,58,73 or bare-gold surfaces. 63,[74][75][76] Some studies using different force fields such as CHARMM [77][78] and OPLS [79][80] for the proteins and SAMS, or GolP 81 and coarse-grain models [82][83] for the gold atoms, thus showing the robustness of molecular simulations approaches for the investigation of protein-surface interactions.…”

Section: β-Glucosidase Position In the Simulation Cellmentioning

confidence: 99%

Between two walls: Modeling the adsorption behavior of β-glucosidase A on bare and SAM-functionalised gold surfaces

Bourassin

Barbault

Baaden

et al. 2021

Preprint

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The efficient immobilization of enzymes on surfaces remains a complex but central issue in the biomaterials field, which requires us to understand this process at the atomic level. Using a multi-scale approach combining all-atom molecular dynamics and coarse-grain Brownian dynamics simulations, we investigated the adsorption behavior of Beta-glucosidase A (BGA) on bare and SAM-functionalized gold surfaces. We monitored the enzyme position and orientation during the MD trajectories, and measured the contacts it forms with both surfaces. While the adsorption process has little impact on the protein conformation, it can nonetheless perturb its mechanical properties and catalytic activity. Our results show that compared to the SAM-functionalized surface, the adsorption of BGA on bare gold is more stable, but also less specific, and more likely to disrupt the enzyme's function. This observation emphasizes the fact that the structural organization of proteins at the solid interface is a keypoint when designing devices based on enzyme immobilization, as one must find an acceptable stability-activity trade-off.

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Interaction of collagen like peptides with gold nanosurfaces: a molecular dynamics investigation

Cited by 28 publications

References 59 publications

Collagen/gold nanoparticle nanocomposites: A potential skin wound healing biomaterial

Collagen/gold nanoparticle nanocomposites: A potential skin wound healing biomaterial

Molecular underpinnings of integrin binding to collagen-mimetic peptides containing vascular Ehlers–Danlos syndrome–associated substitutions

Between two walls: Modeling the adsorption behavior of β-glucosidase A on bare and SAM-functionalised gold surfaces

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