Protein-resistant coatings have been studied for inhibiting biofilm formation on implant devices. In this study, titanium (Ti) surfaces were biofunctionalized with poly(ethylene glycol) (PEG) by electrodeposition and were evaluated as biofilm substrates under an oral simulated environment. Streptococcus gordonii, an early colonizer of oral biofilms, was inoculated on Ti and PEG-electrodeposited Ti (PEG-Ti) surfaces and was analyzed quantitatively and topographically. Streptococcus mutans supplemented with sucrose, a late colonizer mainly found in dental plaque, was also used to form biofilms on the surfaces of Ti and PEG-Ti for 20 h followed by sonication as a means of detaching the biofilms. The results indicated that the attachment of S. gordonii on PEG-Ti surfaces was inhibited compared with Ti, and the S. mutans biofilm was easier to be detached from the surface of PEG-Ti than that of Ti. Moreover, the presence of PEG electrodeposited on Ti surface inhibited salivary protein adsorption. The degree of detachment of biofilms from PEG-Ti was associated with the inhibition of the salivary protein adsorption, suggesting weak basal attachment of the biofilms to the electrodeposited surfaces. Therefore, controlling protein adsorption at the initial stage of biofilm formation may be an effective strategy to protect metal surfaces from bacterial contamination not only in dental manipulations but also in orthopedic applications.

Download full-text PDF

Source
http://dx.doi.org/10.1002/jbm.a.32932DOI Listing

Publication Analysis

Top Keywords

protein adsorption
12
polyethylene glycol
8
biofilm formation
8
peg-ti surfaces
8
salivary protein
8
surfaces
6
biofilm
5
biofilms
5
peg-ti
5
effects electrodeposited
4

Similar Publications

Preparation of the immobilized α-adrenoceptor column by the ultra-high affinity protein pair CL7/Im7 and its application in drug-protein interaction analysis.

J Chromatogr B Analyt Technol Biomed Life Sci

January 2025

Northwest University Chang An Hospital, Faculty of Life Sciences and Medicine, Northwest University, Xi'an, Shaanxi 710069, China; Department of Clinical Pharmaceutics, Chang An District Hospital, Xi'an, Shaanxi 710118, China. Electronic address:

Immobilizing the target protein on a solid surface with controlled orientation, high specificity, and maintained activity is a proven strategy to enhance the stability of the protein. In this study, we employed an ultra-high affinity protein pair consisting of a mutant of colicin E7 Dnase and its corresponding inhibitor, immunity protein 7(Im7), to develop an immobilized α-adrenoceptor (α-AR) column. Briefly, we expressed α-AR fused with CL7 as a tag at its C-terminus in Escherichia coli cells.

View Article and Find Full Text PDF

Experimental and computational analysis of lipophilicity and plasma protein binding properties of potent tacrine based cholinesterase inhibitors.

J Chromatogr B Analyt Technol Biomed Life Sci

January 2025

University of Belgrade-Institute of Chemistry, Technology and Metallurgy, Department of Chemistry, Njegoševa 12, 11000 Belgrade, Republic of Serbia. Electronic address:

The lipophilicity of thirteen tacrine/piperidine-4-carboxamide derivatives was assessed using reversed-phase thin-layer chromatography (RP-TLC) with MeOH and acetonitrile (ACN) as organic modifiers. Among the parameters evaluated, the R and C values obtained using MeOH were identified as the most reliable for characterizing the lipophilicity of the investigated compounds. The observed differences in lipophilicity among the derivatives resulted from a delicate interplay of substituent effects (hydrophobicity, polarity, steric hindrance, and electronic effects), positional influence, and characteristics of the organic modifier.

View Article and Find Full Text PDF

We synthesized rigid, macromolecular brushes with well-defined and quantized brush lengths on a gold nanoparticle substrate by using a macromolecular "grafting from" approach. The macromonomers used in these brushes were thiol- and maleimide-functionalized peptide coiled coil "bundlemers" that fold into discrete 4 nm × 2 nm (length × diameter) cylindrical nanoparticles. With each added peptide macromonomer layer, brush thickness increased by approximately the length of a single bundlemer nanoparticle.

View Article and Find Full Text PDF

Membrane incompatibility poses significant health risks, including severe complications and potential fatality. Surface modification of membranes has emerged as a pivotal technology in the membrane industry, aiming to improve the hemocompatibility and performance of dialysis membranes by mitigating undesired membrane-protein interactions, which can lead to fouling and subsequent protein adsorption. Affinity energy, defined as the strength of interaction between membranes and human serum proteins, plays a crucial role in assessing membrane-protein interactions.

View Article and Find Full Text PDF

Plasmonic Slippery Surface for Surface-Enhanced Raman Spectroscopy and Protein Adsorption Inhibition.

Anal Chem

January 2025

Department of Atomic and Molecular Physics, Manipal Academy of Higher Education, Manipal 576104, India.

Slippery liquid-infused porous surfaces (SLIPSs) are a class of surface that offers low contact angle hysteresis and low tilt angle for water droplet shedding. This property also endows the surface with pinning-free evaporation, which in turn has been exploited for analyte concentration enrichment for Surface Enhanced Raman Spectroscopic applications and antibiofouling. Herein, we demonstrate a facile approach for creating SLIPS with low contact angle hysteresis and low tilt angle for water shedding by coating the equal-volume mixture of polydimethylsiloxane (PDMS) and silicone oil.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!