Scholarly Work - Center for Biofilm Engineering

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    Influence of divalent cations and ph on adsorption of a bacterial polysaccharide adhesin
    (1998-09) Bhosle, N.; Suci, Peter A.; Baty, Ace M.; Weiner, R. M.; Geesey, Gill G.
    Hyphomonas MHS-3 (MHS-3) elaborates a diffuse capsular material, primarily composed of polysaccharide, which has been implicated to serve as the holdfast of this prosthecate marine bacterium. A purified polysaccharide (fr2ps) from this capsular material exhibits a relatively large affinity for (Ge), or more precisely for the Ge oxide surface film. In its natural habitat MHS-3 attaches to marine sediments. This suggests that molecular properties of fr2ps have evolved to render it adhesive toward mineral oxides. In order to characterize these molecular interactions, the effect of divalent cations and pH on the adsorption of fr2ps to Ge has been measured using attenuated total internal reflection Fourier transform infrared (ATR/FT-IR) spectroscopy. The effect of adsorption of fr2ps on the Ge oxide film has been investigated using X-ray photoelectron spectroscopy (XPS). The results indicate that divalent cations participate in binding of fr2ps to Ge oxide and that atomic size of the cation is important. Evidence for significant participation of hydrogen bonding to the oxide surface is lacking.
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    Investigation of interactions between antimicrobial agents and bacterial biofilms using attenuated total reflection fourier transform infrared spectroscopy
    (1998-03) Suci, Peter A.; Vrany, Julia Dawn; Mittelman, M. W.
    Biomaterial-centred infections are often difficult to treat. An impaired immune response, acute inflamatory reactions and the presence of recalcitrant attached microorganisms are all contributing factors. A brief review of the role of attached bacteria in biomaterial-centred infections is presented. Two major hypotheses which may explain the recalcitrance of biofilms to antimicrobial agents are discussed. The analytical capabilities of attenuated total reflection Fourier transform infrared (ATR/FTIR) spectroscopy for providing information on both transport of an antimicrobial agent to bacteria embedded in the biofilm and interactions between an antimicrobial agent and biofilm components are described.
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    Characterization of extracellular chitinolytic activity in biofilms
    (2001) Baty, Ace M.; Diwu, Zhenjun; Dunham, G.; Eastburn, Callie C.; Geesey, Gill G.; Goodman, Amanda E.; Suci, Peter A.; Techkarnjanaruk, Somkiet
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    Adsorption of adhesive proteins from the marine mussel, mytilus edulis, on polymer films in the hydrated state using angle dependent x-ray photoelectron spectroscopy and atomic force microscopy
    (1997-10) Baty, Ace M.; Leavitt, P. K.; Siedlecki, C. A.; Tyler, Bonnie J.; Suci, Peter A.; Marchant, R. E.; Geesey, Gill G.
    The adsorption of mussel adhesive protein (MAP) from the marine mussel Mytilus edulis has been investigated on polystyrene (PS) and poly(octadecyl methacrylate) (POMA) surfaces using angle dependent X-ray photoelectron spectroscopy (XPS) and atomic force microscopy (AFM). AFM images previously published in the dehydrated state using contact mode are compared with images acquired in the hydrated state using fluid Tapping Mode to assess the contribution that hydration has on the architecture of the adsorbed proteins. To further characterize the adsorbed protein layer, XPS analysis was performed at liquid nitrogen (LN2) temperature without dehydrating the samples and at room temperature after the surfaces were dehydrated. The differences observed upon dehydration can be attributed to the strength of the interactions between MAP and the two surfaces. The AFM and XPS data indicate that adsorbed MAP is stabilized on the surface of the PS through interactions that prevent the protein layer from being disrupted upon dehydration. The adsorbed MAP on the POMA surface is representative of a loosely bound protein layer that becomes highly perturbed upon dehydration.
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    Adhesion of biofilms to inert surfaces: a molecular level approach directed at the marine environments
    (1996-09) Baty, Ace M.; Frolund, B.; Geesey, Gill G.; Langille, S. E.; Quintero, Ernesto J.; Suci, Peter A.; Weiner, R. M.
    Protein/ligand interactions involved in mediating adhesion between microorganisms and biological surfaces have been well‐characterized in some cases (e.g. pathogen/host interactions). The strategies microorganisms employ for attachment to inert surfaces have not been so clearly elucidated. An experimental approach is presented which addresses the issues from the point of view of molecular interactions occurring at the interface.
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    Influence of protein conditioning films on binding of a bacterial polysaccharide adhesin from hyphomonas mhs-3
    (1996-09) Frolund, B.; Suci, Peter A.; Langille, S. E.; Weiner, R. M.; Geesey, Gill G.
    A putative polysaccharide adhesin which mediates non‐specific attachment of Hyphomonas MHS‐3 (MHS‐3) to hydrophilic substrata has been isolated and partially characterized. A polysaccharide‐enriched portion of the extracellular polymeric substance (EPSP) from MHS‐3 was separated into four fractions using high performance size exclusion chromatography (HPSEC). Comparison of chromatograms of EPSP from MHS‐3 and a reduced adhesion strain (MHS‐3 rad) suggested that one EPSP fraction, which consisted of carbohydrate, served as an adhesin. Adsorption of this fraction to germanium (Ge) was investigated using attenuated total reflection Fourier transform infrared (ATR/FT‐IR) spectrometry. Binding curves indicated that the isolated fraction had a relatively high affinity for Ge when ranked against an adhesive protein from Mytilis edulis, mussel adhesive protein (MAP) and an acidic polysaccharide (alginate from Macrocystis pyrifera). Spectral features were used to identify the fraction as a polysaccharide previously reported to adsorb preferentially out of the EPSP mixture. Conditioning the Ge substratum with either bovine serum albumin (BSA) or MAP decreased the adsorption of the adhesive polysaccharide significantly. Conditioning Ge with these proteins also decreased adhesion of whole cells.
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    Investigation of mussel adhesive protein adsorption on polystryene and poly(octadecyl methacrylate) using angle dependent xps, atr-ftir and afm
    (1996-02) Baty, Ace M.; Suci, Peter A.; Tyler, Bonnie J.; Geesey, Gill G.
    The irreversible adsorption of mussel adhesive proteins (MAP) from the marine mussel Mytilus edulishas been investigated on polystyrene (PS) and poly(octadecyl methacrylate) (POMA) surfaces using angle resolved X-ray photoelectron spectroscopy (XPS), attenuated total reflection Fourier transform infrared (ATR-FTIR) spectrometry, and atomic force microscopy (AFM). Angle resolved XPS was used to quantify the elemental composition with depth of the upper 90 Å of the surface, and AFM was used to obtain the surface topography. The adsorption pattern of MAP, revealed by AFM images, is distinctly different on the two polymer surfaces and suggests that the substratum influences protein adhesion. The depth profiles of MAP, obtained from angle resolved XPS, show differences in nitrogen composition with depth for MAP adsorbed to PS and POMA. Infrared spectra of hydrated adsorbed MAP revealed significant differences in the amide III region and in two bands which may originate from residues in the tandemly repeated sequences of MAP. This data demonstrates that the chemistry of the polymer film that is present at the protein–polymer interface can influence protein–protein and protein–surface interactions.
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    Adhesive extracellular polymers of hyphomonas mhs-3: interaction of polysaccharides and proteins
    (1995-12) Suci, Peter A.; Frolund, B.; Quintero, Ernesto J.; Weiner, R. M.; Geesey, Gill G.
    The adsorption behavior of extracellular polymeric substances (EPS) from the marine bacterium Hyphomonas MHS‐3 was investigated using attenuated total reflection Fourier transform infrared (ATR/FT‐IR) spectrometry. The protein fraction of the crude EPS (EPSC) (propanol precipitated/extracted with EDTA) dominated the adsorption onto the germanium substratum. Removal of the Protease K accessible portion of the EPSC protein, and treatment with RNase and DNase, yielded a hygroscopic substance (EPSP) which contained at least one adhesive polysaccharide component. Conditioning the substratum with EPSC diminished adsorption of the polysaccharide fractions in EPSP; pre‐adsorbed EPSC protein was not displaced. The rate of EPSC adsorption on substrata conditioned with EPSP was slower than to clean germanium; however, the projected surface coverage of protein after long times, based on an empirical datafit, was the same as that for a clean substratum; the EPSC proteins did not displace the pre‐adsorbed adhesive polysaccharide fraction. SDS‐PAGE (Coomassie blue stain) revealed an extensive homology between proteins from cell lysates and EPSC proteins. However, distinct differences in the banding pattern suggested that proteins did not originate primarily from cell lysis during the extraction procedure. The results indicate that adhesive components of EPS, with respect to a hydrophilic surface (germanium), can be either protein or polysaccharide and that they may compete for interfacial binding sites.
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