Surface modification mediates the interaction between fullerene and lysozyme: protein structure and antibacterial activity

Bai, Yitong; Wu, Xian; Ouyang, Peng; Shi, M.; Li, Qun; Maimaiti, Tusunniyaze; Lan, Suke; Yang, Shengrong; Chang, Xueling

doi:10.1039/d0en00645a

Cited by 20 publications

(13 citation statements)

References 55 publications

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“…If we consider the extended π-system of the fullerene, it is not surprising that aromatic amino acids such as tryptophan, tyrosine, phenylalanine, and histidine interacted the most with it ( Figure 3 ) [ 20 , 24 , 33 , 34 , 35 , 39 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 ]. In particular, Trp exhibited the largest value of binding energy among the twenty proteinogenic amino acids.…”

Section: Resultsmentioning

confidence: 99%

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Dissecting the Supramolecular Dispersion of Fullerenes by Proteins/Peptides: Amino Acid Ranking and Driving Forces for Binding to C60

Marforio

Calza

Mattioli

et al. 2021

IJMS

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Molecular dynamics simulations were used to quantitatively investigate the interactions between the twenty proteinogenic amino acids and C60. The conserved amino acid backbone gave a constant energetic interaction ~5.4 kcal mol−1, while the contribution to the binding due to the amino acid side chains was found to be up to ~5 kcal mol−1 for tryptophan but lower, to a point where it was slightly destabilizing, for glutamic acid. The effects of the interplay between van der Waals, hydrophobic, and polar solvation interactions on the various aspects of the binding of the amino acids, which were grouped as aromatic, charged, polar and hydrophobic, are discussed. Although π–π interactions were dominant, surfactant-like and hydrophobic effects were also observed. In the molecular dynamics simulations, the interacting residues displayed a tendency to visit configurations (i.e., regions of the Ramachandran plot) that were absent when C60 was not present. The amino acid backbone assumed a “tepee-like” geometrical structure to maximize interactions with the fullerene cage. Well-defined conformations of the most interactive amino acids (Trp, Arg, Met) side chains were identified upon C60 binding.

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Section: Resultsmentioning

confidence: 99%

“…Experimentally, in C 60 @lysozyme, π-stacking interactions between C 60 and Trp (sandwich-like for Trp62 and T-shape-like for Trp63) are crucial for binding [ 24 , 35 , 51 ]. Analogously, in a peptide designed to recognize C 60 , C 60 is wedged between two Tyr residues [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

Dissecting the Supramolecular Dispersion of Fullerenes by Proteins/Peptides: Amino Acid Ranking and Driving Forces for Binding to C60

Marforio

Calza

Mattioli

et al. 2021

IJMS

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“…It is known that fullerenes have high bacteriostatic properties not only against E. coli bacteria, but also against bacteria B. subtilis, S. Aureus, S. epidermidis, E. hirae, S. typhi, P. acnes, and E. faecalis [11][12][13][78][79][80][81][82][83][84][85]. The use of borosiloxane as a carrier increases the detachment of bacteria from the substrate by one order of magnitude, and the incorporation of 0.1 wt% fullerenes decreases the density of bacterial structures by 3 times (under light irradiation) and increases the detachment of bacteria five-fold.…”

Section: Discussionmentioning

confidence: 99%

Novel Biocompatible with Animal Cells Composite Material Based on Organosilicon Polymers and Fullerenes with Light-Induced Bacteriostatic Properties

et al. 2021

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A technology for producing a nanocomposite based on the borsiloxane polymer and chemically unmodified fullerenes has been developed. Nanocomposites containing 0.001, 0.01, and 0.1 wt% fullerene molecules have been created. It has been shown that the nanocomposite with any content of fullerene molecules did not lose the main rheological properties of borsiloxane and is capable of structural self-healing. The resulting nanomaterial is capable of generating reactive oxygen species (ROS) such as hydrogen peroxide and hydroxyl radicals in light. The rate of ROS generation increases with an increase in the concentration of fullerene molecules. In the absence of light, the nanocomposite exhibits antioxidant properties. The severity of antioxidant properties is also associated with the concentration of fullerene molecules in the polymer. It has been shown that the nanocomposite upon exposure to visible light leads to the formation of long-lived reactive protein species, and is also the reason for the appearance of such a key biomarker of oxidative stress as 8-oxoguanine in DNA. The intensity of the process increases with an increase in the concentration of fullerene molecules. In the dark, the polymer exhibits weak protective properties. It was found that under the action of light, the nanocomposite exhibits significant bacteriostatic properties, and the severity of these properties depends on the concentration of fullerene molecules. Moreover, it was found that bacterial cells adhere to the surfaces of the nanocomposite, and the nanocomposite can detach bacterial cells not only from the surfaces, but also from wetted substrates. The ability to capture bacterial cells is primarily associated with the properties of the polymer; they are weakly affected by both visible light and fullerene molecules. The nanocomposite is non-toxic to eukaryotic cells, the surface of the nanocomposite is suitable for eukaryotic cells for colonization. Due to the combination of self-healing properties, low cytotoxicity, and the presence of bacteriostatic properties, the nanocomposite can be used as a reusable dry disinfectant, as well as a material used in prosthetics.

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“… ,− With the increase of the carbon cage size, the binding strength between proteins and fullerenes increases constantly. , Then the local interactions between the amino acids and the fullerenes come into play. The amino acids most effectively interacting with fullerenes are aromatic residues (tryptophan, phenylalanine, tyrosine, and histidine) that can establish π–π stacking interactions with the cage (Figure a,b). ,,,− In C 60 @lysozyme and C 70 @lysozyme, π-stacking interactions are sandwich-like for Trp62 and T-shape-like for Trp63 (Figure a). ,,− In the design of peptides/proteins able to recognize C 60 (i.e., COP, C 60 -organizing peptide), the π–π aromatic stacking between C 60 and tyrosines (Figure b) is the driving force in the binding process. , In fact, C 60 is wedged between two Tyr residues.…”

Section: Protein–mnp Interfacementioning

confidence: 99%

“…A second alternative are fullerene derivatives (FDs). Functionalization is usually carried out to improve solubility, and upon protein binding, an energy penalty is paid for the desolvation of the hydrophilic functional groups. , A high degree of chemical functionalization generally reduces the π–π interactions, while slightly increasing other interactions such as hydrogen bond, results in an overall weaker binding strength. , A systematic analysis of the interaction between FDs and proteins demonstrated that proteins showing high binding interact more strongly with FDs because of hydrophobic interactions of the proteins with fullerene core. In the crystal structure of COP and fullerene derivatives, the water-solubilizing tris-acid side chain of C 60 is not visible in the electron density map, due to its mobility, whereas the C 60 core appears responsible for the packing arrangement.…”

Section: Protein–mnp Interfacementioning

confidence: 99%

Incorporation of Molecular Nanoparticles Inside Proteins: The Trojan Horse Approach in Theranostics

2021

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Metrics & MoreArticle Recommendations CONSPECTUS: Molecular nanoparticles, MNPs, characterized by well-defined chemical formulas, structures, and sizes can interact with a variety of proteins. Fullerenes, carboranes, and gold nanoclusters well represent the diversity of MNPs properties available in nanoscience. They can have diameters smaller than 1.5 nm, be hydrophilic or hydrophobic, and can use a paraphernalia of means to establish local and global interactions with the amino acidic residues of proteins. Proteins, endowed as they are with an assortment of pockets, crevices, and gaps are natural supramolecular hosts to incorporate/hide/transport MNPs directly in water with a facile and "green" approach. This Account identifies and discusses the rules that govern the interactions and binding between MNPs and proteins. Fullerenes are composed solely by carbon atoms arranged to form hollow polyhedra. Hydrophobic interactions occur between aliphatic residues and the fullerene surface. The amino acids most effectively interacting with fullerenes are aromatic residues that establish π−π stacking interactions with the cage. Amphiphilic and charged residues produce also cation−π, anion−π, and surfactant-like interactions with the cages.Carboranes are composed of boron, carbon, and hydrogen atoms, also arranged to form cages. They are hydrophobic with unusual properties originating from the presence of boron atoms. Hydride-like hydrogens bound to the boron atoms govern carborane chemistry. These negatively charged hydrogens do not participate in classic hydrogen bonding with water and promote hydrophobic interactions with proteins. On the contrary, the electronegativity of these hydrogens drives the formation of unconventional dihydrogen bonds with the acidic hydrogen atoms of positively charged amino acid. Carboranes also establish C−H•••π and B−H•••π interactions with aromatic residues. Gold nanoclusters, AuNCs, are synthesizable with atomically precise stoichiometry. Amino acid residues with sulfur atoms or with nitrogen-containing heterocycles are the strongest Au binders. The proteins can act as supramolecular hosts but also as templates for the synthesis of AuNCs directly inside the protein core. Of the pristine amino acids, tryptophan, tyrosine, phenylalanine, and aspartic acid are the most efficient reducing groups. In a peptide sequence, the best Au-reducing moieties are obtained by nitrogencontaining residue such as glutamine, asparagine, arginine, and lysine. The investigation of the interactions between AuNCs and proteins therefore adds further complexity with respect to that of fullerenes and carboranes. The selection of the host proteins should consider that they will have to contain active sites for metal ion accumulation and ion reduction where AuNC can form and stabilize. This Account further discusses the hybridization of MNPs with proteins in view of creating innovative multifunctional theranostic platforms where the role of proteins is akin to that of "Trojan Horses" since they can (i) hide the MNPs,...

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Surface modification mediates the interaction between fullerene and lysozyme: protein structure and antibacterial activity

Abstract: Chemical functionalization is widely adopted to increase the hydrophilicity of fullerene for various applications. Protein-nanomaterials (NM) interaction is one of the very first issues after NMs enter biological systems, which...

Cited by 20 publications

References 55 publications

Dissecting the Supramolecular Dispersion of Fullerenes by Proteins/Peptides: Amino Acid Ranking and Driving Forces for Binding to C60

Dissecting the Supramolecular Dispersion of Fullerenes by Proteins/Peptides: Amino Acid Ranking and Driving Forces for Binding to C60

Novel Biocompatible with Animal Cells Composite Material Based on Organosilicon Polymers and Fullerenes with Light-Induced Bacteriostatic Properties

Incorporation of Molecular Nanoparticles Inside Proteins: The Trojan Horse Approach in Theranostics

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