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      A biomimetic anti-biofouling coating in nanofluidic channels

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          Abstract

          A biomimetic coating using a tailored phosphorylcholine-containing monomer enables to suppress non-specific protein adsorption in nanofluidic channels, paving a way to explore a new anti-biofouling strategy using monomer-based materials for nanodevices.

          Abstract

          Non-specific protein adsorption (NPA) is ubiquitous and generally considered a trigger for various biofoulings, adversely affecting diverse fields. Despite many approaches (generally polymer-based) available to combat NPA in a wide range of length scales, suppressing NPA in closed nanoscale spaces of emerging nanodevices such as nanofluidic devices remains a challenge due to the lack of suitable material and methodology to satisfy their ultra-small and closed features. In this study, a biomimetic, hydrosilane-functionalized 2-methacryloyloxyethyl phosphorylcholine (MPC) monomer material, which has tailored molecular characteristics and well-defined surface properties to overcome the challenges in the nanospaces, is elaborately designed and synthesized to form self-assembled, nanoscale, biomimetic coatings, enabling the efficient suppression of NPA in femtoliter-order, closed nanofluidic channels. The approach opens up a new path for exploring a strategic change of anti-biofouling coating from traditional polymer-based methodologies to a monomer-based methodology to overcome the challenge of suppressing NPA in closed nanospaces.

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          Measurement of protein using bicinchoninic acid

          P.K. Smith, R.I. Krohn, G.T. Hermanson … (1985)
          Bicinchoninic acid, sodium salt, is a stable, water-soluble compound capable of forming an intense purple complex with cuprous ion (Cu1+) in an alkaline environment. This reagent forms the basis of an analytical method capable of monitoring cuprous ion produced in the reaction of protein with alkaline Cu2+ (biuret reaction). The color produced from this reaction is stable and increases in a proportional fashion over a broad range of increasing protein concentrations. When compared to the method of Lowry et al., the results reported here demonstrate a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts. The stability of the reagent and resulting chromophore also allows for a simplified, one-step analysis and an enhanced flexibility in protocol selection. This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique.
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            Antifouling coatings: recent developments in the design of surfaces that prevent fouling by proteins, bacteria, and marine organisms.

            Indrani Banerjee, Ravindra Pangule, Ravi Kane (2011)
            The major strategies for designing surfaces that prevent fouling due to proteins, bacteria, and marine organisms are reviewed. Biofouling is of great concern in numerous applications ranging from biosensors to biomedical implants and devices, and from food packaging to industrial and marine equipment. The two major approaches to combat surface fouling are based on either preventing biofoulants from attaching or degrading them. One of the key strategies for imparting adhesion resistance involves the functionalization of surfaces with poly(ethylene glycol) (PEG) or oligo(ethylene glycol). Several alternatives to PEG-based coatings have also been designed over the past decade. While protein-resistant coatings may also resist bacterial attachment and subsequent biofilm formation, in order to overcome the fouling-mediated risk of bacterial infection it is highly desirable to design coatings that are bactericidal. Traditional techniques involve the design of coatings that release biocidal agents, including antibiotics, quaternary ammonium salts (QAS), and silver, into the surrounding aqueous environment. However, the emergence of antibiotic- and silver-resistant pathogenic strains has necessitated the development of alternative strategies. Therefore, other techniques based on the use of polycations, enzymes, nanomaterials, and photoactive agents are being investigated. With regard to marine antifouling coatings, restrictions on the use of biocide-releasing coatings have made the generation of nontoxic antifouling surfaces more important. While considerable progress has been made in the design of antifouling coatings, ongoing research in this area should result in the development of even better antifouling materials in the future. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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              Interpretation of protein adsorption: surface-induced conformational changes.

              Paul Roach, David T. Farrar, Carole C. Perry (2005)
              Protein adhesion plays a major role in determining the biocompatibility of materials. The first stage of implant integration is the adhesion of protein followed by cell attachment. Surface modification of implants (surface chemistry and topography) to induce and control protein and cell adhesion is currently of great interest. This communication presents data on protein adsorption (bovine serum albumin and fibrinogen) onto model hydrophobic (CH(3)) and hydrophilic (OH) surfaces, investigated using a quartz crystal microbalance (QCM) and grazing angle infrared spectroscopy. Our data suggest that albumin undergoes adsorption via a single step whereas fibrinogen adsorption is a more complex, multistage process. Albumin has a stronger affinity toward the CH(3) compared to OH terminated surface. In contrast, fibrinogen adheres more rapidly to both surfaces, having a slightly higher affinity toward the hydrophobic surface. Conformational assessment of the adsorbed proteins by grazing angle infrared spectroscopy (GA-FTIR) shows that after an initial 1 h incubation few further time-dependent changes are observed. Both proteins exhibited a less organized secondary structure upon adsorption onto a hydrophobic surface than onto a hydrophilic surface, with the effect observed greatest for albumin. This study demonstrates the ability of simple tailor-made monochemical surfaces to influence binding rates and conformation of bound proteins through protein-surface interactions. Current interest in biocompatible materials has focused on surface modifications to induce rapid healing, both of implants and for wound care products. This effect may also be of significance at the next stage of implant integration, as cell adhesion occurs through the surface protein layer.
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                Author and article information

                Contributors
                Journal
                Journal ID (publisher-id): JMCBDV
                Title: Journal of Materials Chemistry B
                Abbreviated Title: J. Mater. Chem. B
                Publisher: Royal Society of Chemistry (RSC)
                ISSN (Print): 2050-750X
                ISSN (Electronic): 2050-7518
                Publication date Created: April 06 2022
                Publication date (Electronic): 2022
                Volume: 10
                Issue: 14
                Pages: 2481-2489
                Affiliations
                [1 ]Department of Chemical Engineering, Graduate School of Engineering, Osaka Prefecture University, 1-2, Gakuen-cho, Naka-ku, Sakai, Osaka 599-8570, Japan
                [2 ]Department of Chemistry, Graduate School of Science, Osaka Prefecture University, 1-1, Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan
                [3 ]Japan Science and Technology Agency (JST), PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan
                [4 ]NanoSquare Research Institute, Research Center for the 21st Century, Organization for Research Promotion, Osaka Prefecture University, 1-2, Gakuen-cho, Naka-ku, Sakai, Osaka 599-8570, Japan
                Article
                DOI: 10.1039/D1TB02627E
                PubMed ID: 35072197
                SO-VID: bae3e802-c7b4-4abf-a154-9db6c1ca522b
                Copyright © © 2022
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                http://rsc.li/journals-terms-of-use#chorus

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