Promotion of fibroblast activity by coating with hydrophobins in the β-sheet end state

Janssen, Meike; Leeuwen, M. B. M. van; Kooten, van Theo; Vries, de Alex; Dijkhuizen, Lubbert; Wösten, Han A. B.

doi:10.1016/j.biomaterials.2003.09.060

Cited by 76 publications

(62 citation statements)

References 32 publications

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“…As a result, adherence of soil bacteria and fungi may be stimulated or decreased. For example, growth and adherence of fibroblasts to Teflon could be improved by coating a hydrophobic solid with hydrophobins Janssen et al 2002Janssen et al , 2004. Enzymes secreted by microorganisms may also be stabilized by the hydrophobin film.…”

Section: Hydrophobinsmentioning

confidence: 98%

Role of proteins in soil carbon and nitrogen storage: controls on persistence

et al. 2007

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Mechanisms of soil organic carbon (C) and nitrogen (N) stabilization are of great interest, due to the potential for increased CO 2 release from soil organic matter (SOM) to the atmosphere as a result of global warming, and because of the critical role of soil organic N in controlling plant productivity. Soil proteins are recognized increasingly as playing major roles in stabilization and destabilization of soil organic C and N. Two categories of proteins are proposed: detrital proteins that are released upon cell death and functional proteins that are actively released into the soil to fulfill specific functions. The latter include microbial surface-active proteins (e.g., hydrophobins, chaplins, SC15, glomalin), many of which have structures that promote their persistence in the soil, and extracellular enzymes, responsible for many decomposition and nutrient cycling transformations. Here we review information on the nature of soil proteins, particularly those of microbial origin, and on the factors that control protein persistence and turnover in the soil. We discuss first the intrinsic properties of the protein molecule that affect its stability, next possible extrinsic stabilizing influences that arise as the proteins interact with other soil constituents, and lastly controls on accessibility of proteins at coarser spatial scales involving microbial cells, clay particles, and soil aggregates. We conclude that research at the interface between soil science and microbial physiology will yield rapid advances in our understanding of soil proteins. We suggest as research priorities determining the relative abundance and turnover time (age) of microbial versus plant proteins and of functional microbial proteins, including surfaceactive compounds.

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Section: Hydrophobinsmentioning

confidence: 98%

Role of proteins in soil carbon and nitrogen storage: controls on persistence

et al. 2007

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“…Such films can reverse the wettability of a surface such Teflon and are considered to have great potential as biomaterials (14,15). However, despite considerable efforts, our knowledge of the structure of hydrophobins and the mechanism through which they form rodlets is far from complete.…”

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confidence: 99%

Structural basis for rodlet assembly in fungal hydrophobins

Kwan

Winefield

Sunde

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

224

247

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Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are formed. There are also significant similarities between these polymers and amyloid-like fibrils. However, structural information on these proteins and the rodlets they form has been elusive. Here, we describe the three-dimensional structure of the monomeric form of the class I hydrophobin EAS. EAS forms a ␤-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface. This structure is consistent with its ability to form an amphipathic polymer. By using this structure, together with data from mutagenesis and previous biophysical studies, we have been able to propose a model for the polymeric rodlet structure adopted by these proteins. X-ray fiber diffraction data from EAS rodlets are consistent with our model. Our data provide molecular insight into the nature of hydrophobin rodlet films and extend our understanding of the fibrillar ␤-structures that continue to be discovered in the protein world. amyloid ͉ NMR ͉ polymer H ydrophobins are a large family of secreted, low-molecularmass (7-9 kDa) proteins unique to filamentous fungi. There is little amino acid sequence similarity between hydrophobins, except for a characteristic pattern of eight cysteine residues that form four intramolecular disulfide bonds (1, 2). These proteins have remarkable biophysical properties and function by selfassembling into amphipathic polymeric films at the interface between hydrophobic and hydrophilic surfaces (3). The surfactive and amphipathic properties of hydrophobins facilitate the formation of essential aerial structures such as hyphae, spores, and fruiting bodies (4).Two classes of hydrophobins have been identified based on their hydrophobicity plots and physical properties (5). For class I hydrophobins, the polymer film comprises cylindrical rodlets with dimensions of Ϸ10 ϫ 100-250 nm and their outward-facing hydrophobic surface has extremely low wettability (6, 7). These films are very robust; they are resistant to boiling in detergents or strong alkalis (8, 9). The morphology of isolated rodlets is reminiscent of amyloid fibrils isolated from diseased tissue and formed in vitro. Reconstituted rodlets stained with Congo red give the green-gold birefringence characteristic of similarly stained amyloid fibers and circular dichroism (CD) data indicate that the rodlets contain extensive ␤-structure, suggesting that rodlets and amyloid fibrils have structural features in common (10, 11, **). Class II hydrophobin films are significantly less robust and lack the rodlet morphology of class I hydrophobins (12, 13).Class I hydrophobins, once solubilized, will spo...

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“…For example, hydrophobic surfaces presumably decelerate primary interactions with aqueous bio-systems. Thus, biomaterial surfaces with moderate hydrophilic properties improve cell growth and increase biocompatibility [22].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Biomimetic Coatings on Femtosecond Laser Treated Alumina and Alumina-Zirconia Composite Surfaces

Aguiar

Lima

Braga

et al. 2016

Machining, Joining and Modifications of Advanced Materials

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The effect of texturing Al 2 O 3 and Al 2 O 3 /ZrO 2 surfaces using femtosecond laser has been evaluated in terms of the roughness, wettability and microstructure of the substrate to increase growth efficiency and adhesion of hydroxyapatite. Femtosecond laser treatment of these materials causes phase transformation from alpha-alumina to gamma-alumina. Heat effects during femtosecond laser treatment causes the grains to be in the nanometer scale. Without heat effects, the grains are in the micrometer scale. The use of femtosecond laser permits control of the surface roughness of the alumina specimens. The higher the femtosecond laser energy, the higher is the wettability of the specimen and the total surface energy. Specimens with laser textured surfaces upon immersion in 1.5 SBF for 6 and 15 days revealed apatite layers well bonded to the substrate and without detachment. The adhesion of apatite to surfaces of specimens that were not textured with femtosecond laser was inadequate.

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Promotion of fibroblast activity by coating with hydrophobins in the β-sheet end state

Cited by 76 publications

References 32 publications

Role of proteins in soil carbon and nitrogen storage: controls on persistence

Role of proteins in soil carbon and nitrogen storage: controls on persistence

Structural basis for rodlet assembly in fungal hydrophobins

Evaluation of Biomimetic Coatings on Femtosecond Laser Treated Alumina and Alumina-Zirconia Composite Surfaces

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