Adsorption properties of albumin and fibrinogen on hydrophilic/hydrophobic TiO2 surfaces: A molecular dynamics study

Wu, Xiao; Wang, Chenyang; Hao, Pengfei; He, Feng; Yao, Zhaohui; Zhang, Xiwen

doi:10.1016/j.colsurfb.2021.111994

Cited by 19 publications

(14 citation statements)

References 56 publications

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“…Likewise, the flexible ratio of arginine (R) in the nonstrict case and aspartic (D) in the strict case are higher values. This discovery can be supported by previous studies on protein flexibility 14,42 . Although proteins with more hydrophilic amino acids in the molecule are relatively more flexible in the aqueous environment, in Figures 2 and 3 cysteines (C) appear too much in the rigid regions, which is due to the possibility of rigid disulfide bond is formed between them 43,44 .…”

Section: Discussionsupporting

confidence: 59%

“…This discovery can be supported by previous studies on protein flexibility. 14 , 42 Although proteins with more hydrophilic amino acids in the molecule are relatively more flexible in the aqueous environment, in Figures 2 and 3 cysteines (C) appear too much in the rigid regions, which is due to the possibility of rigid disulfide bond is formed between them. 43 , 44 Previous studies confirmed the intuition that glycines (G) are flexible, 12 , 45 but we found in more detail that glycine (G) may also present a higher proportion in the rigid region in Figures 2 and 3 .…”

Section: Discussionmentioning

confidence: 99%

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PredictingDNA‐binding protein and coronavirus protein flexibility using protein dihedral angle and sequence feature

Wang

Liu

et al. 2022

Proteins

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The flexibility of protein structure is related to various biological processes, such as molecular recognition, allosteric regulation, catalytic activity, and protein stability. At the molecular level, protein dynamics and flexibility are important factors to understand protein function. DNA‐binding proteins and Coronavirus proteins are of great concern and relatively unique proteins. However, exploring the flexibility of DNA‐binding proteins and Coronavirus proteins through experiments or calculations is a difficult process. Since protein dihedral rotational motion can be used to predict protein structural changes, it provides key information about protein local conformation. Therefore, this paper introduces a method to improve the accuracy of protein flexibility prediction, DihProFle (Prediction of DNA‐binding proteins and Coronavirus proteins flexibility introduces the calculated dihedral Angle information). Based on protein dihedral Angle information, protein evolution information, and amino acid physical and chemical properties, DihProFle realizes the prediction of protein flexibility in two cases on DNA‐binding proteins and Coronavirus proteins, and assigns flexibility class to each protein sequence position. In this study, compared with the flexible prediction using sequence evolution information, and physicochemical properties of amino acids, the flexible prediction accuracy based on protein dihedral Angle information, sequence evolution information and physicochemical properties of amino acids improved by 2.2% and 3.1% in the nonstrict and strict conditions, respectively. And DihProFle achieves better performance than previous methods for protein flexibility analysis. In addition, we further analyzed the correlation of amino acid properties and protein dihedral angles with residues flexibility. The results show that the charged hydrophilic residues have higher proportion in the flexible region, and the rigid region tends to be in the angular range of the protein dihedral angle (such as the ψ angle of amino acid residues is more flexible than rigid in the range of 91°–120°). Therefore, the results indicate that hydrophilic residues and protein dihedral angle information play an important role in protein flexibility.

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Section: Discussionsupporting

confidence: 59%

Section: Discussionmentioning

confidence: 99%

PredictingDNA‐binding protein and coronavirus protein flexibility using protein dihedral angle and sequence feature

Wang

Liu

et al. 2022

Proteins

View full text Add to dashboard Cite

show abstract

“…The fibrinogen adsorption amounts of the different samples are displayed in Figure 4B . It can be seen that more fibrinogen can be adsorbed on the pristine titanium surface because fibrinogen tends to be adsorbed on the hydrophobic surface ( Wu et al, 2021 ). The fibrinogen concentration adsorbed on the TNT surface decreased rapidly because the hydrophilicity was significantly improved after the anodization.…”

Section: Resultsmentioning

confidence: 99%

Construction of Mussel-Inspired Dopamine–Zn2+ Coating on Titanium Oxide Nanotubes to Improve Hemocompatibility, Cytocompatibility, and Antibacterial Activity

Zhou

Liu

et al. 2022

Front. Bioeng. Biotechnol.

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Zinc ions (Zn2+) are a highly potent bioactive factor with a broad spectrum of physiological functions. In situ continuous and controllable release of Zn2+ from the biomaterials can effectively improve the biocompatibility and antibacterial activity. In the present study, inspired by the adhesion and protein cross-linking in the mussel byssus, with the aim of improving the biocompatibility of titanium, a cost-effective one-step metal–catecholamine assembly strategy was developed to prepare a biomimetic dopamine–Zn2+ (DA-Zn2+) coating by immersing the titanium oxide nanotube (TNT) arrays on the titanium surface prepared by anodic oxidation into an aqueous solution containing dopamine (DA) and zinc ions (Zn2+). The DA-Zn2+ coatings with the different zinc contents exhibited excellent hydrophilicity. Due to the continuous release of zinc ions from the DA-Zn2+ coating, the coated titanium oxide nanotubes displayed excellent hemocompatibility characterized by platelet adhesion and activation and hemolysis assay. Moreover, the DA-Zn2+-coated samples exhibited an excellent ability to enhance endothelial cell (EC) adhesion and proliferation. In addition, the DA-Zn2+ coating can also enhance the antibacterial activity of the nanotubes. Therefore, long-term in situ Zn2+-releasing coating of the present study could serve as the bio-surfaces for long-term prevention of thrombosis, improvement of cytocompatibility to endothelial cells, and antibacterial activity. Due to the easy operation and strong binding ability of the polydopamine on various complicated shapes, the method of the present study can be further applied to other blood contact biomaterials or implantable medical devices to improve the biocompatibility.

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“…LYS with molecule weight ( M w ) of 14 kDa was straightforward to deposit on the surface gap of the coatings 47 . Meanwhile, the repulsive force between LYS was less than the proteins like BFG ( M w = 130 kDa), 48 which has more potential binding sites with the material due to its complex composition 49 . PU‐PDA/PHMG surface was positively charged due to the positive charged guanidine group of PHMG.…”

Section: Resultsmentioning

confidence: 99%

Construction of antifouling and antibacterial polyhexamethylguanidine/chondroitin sulfate coating on polyurethane surface based on polydopamine rapid deposition

Zhu

Yuan

Zhang

et al. 2022

J of Applied Polymer Sci

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Implanted medical devices are widely used in clinic for disease treatment, but they generally suffer from the bio‐fouling problem which leads to the reduction of service life and loss of therapeutic effects. Herein, an eco‐friendly method based on polydopamine (PDA) fast deposition is developed to construct anti‐fouling and antibacterial surface on polyurethane (PU). The self‐adhesive layer of PDA contributes to the formation of a platform with active sites for further antibacterial and hydrophilic modification. Polyhexamethylguanidine (PHMG) as antibacterial ingredient and chondroitin sulfate (CS) as hydrophilic component covalently bind on PDA platform, which successively helps to form PU‐PDA/PHMG/CS. The resultant surface demonstrates the excellent property of anti‐protein adsorption (96.8%), anti‐bacterial ability (99.9%), and cell compatibility (95.0%), which would have great potential for medical application.

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Adsorption properties of albumin and fibrinogen on hydrophilic/hydrophobic TiO2 surfaces: A molecular dynamics study

Cited by 19 publications

References 56 publications

PredictingDNA‐binding protein and coronavirus protein flexibility using protein dihedral angle and sequence feature

PredictingDNA‐binding protein and coronavirus protein flexibility using protein dihedral angle and sequence feature

Construction of Mussel-Inspired Dopamine–Zn2+ Coating on Titanium Oxide Nanotubes to Improve Hemocompatibility, Cytocompatibility, and Antibacterial Activity

Construction of antifouling and antibacterial polyhexamethylguanidine/chondroitin sulfate coating on polyurethane surface based on polydopamine rapid deposition

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