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Fungal Influence on Hydrophobic Organic Pollutants Dynamics within the Soil Matrices
Published in Vivek Kumar, Rhizomicrobiome Dynamics in Bioremediation, 2021
Claire Baranger, Isabelle Pezron, Anne Le Goff, Antoine Fayeulle
Filamentous fungi are known to produce extracellular surface-active proteins called hydrophobins that regulate fungal interactions with surfaces and air/water interfaces. Hydrophobins are a family of small cystein-rich proteins (< 15 kDa) displaying both a hydrophilic and a hydrophobic domains, confering them their surfactant properties. By self-assembling into amphiphilic layers at hydrophilic/hydrophobic interfaces, they lower interfacial tension and allow fungal hyphae to break through air/water interfaces as well as attach to hydrophobic substrates (Wösten et al. 1999). Hydrophobins are divided in two classes with differing structures and displaying various biological functions (Table 1). Class I hydrophobins, defined after the CS3 hydrophobin from Schizophyllum commune, form insoluble and extremely stable rodlets. Class II hydrophobins like HFBI and HFBII from Trichoderma reesei self-assemble at interfaces into monolayers (Szilvay et al. 2007, Linder 2009). Hydrophobins are the most potent surfactant proteins known to this day (Wösten 2001, Berger and Sallada 2019): class II hydrophobins from T. reesei are able to lower the surface tension in water phases to up to 25 mN·m–1, and are active at concentrations in the order of 0.1 µmol.L–1 (Cox et al. 2007). They have also been shown to stabilize oil-in-water emulsions and foams (Lumsdon et al. 2005, Tchuenbou-Magaia et al. 2009, Lohrasbi-Nejad et al. 2016).
Biomolecular Modeling in Biomaterials
Published in Heather N. Hayenga, Helim Aranda-Espinoza, Biomaterial Mechanics, 2017
Sai J. Ganesan, Silvina Matysiak
The most commonly recognized β-sheet fibrillar material is an amyloid-like structure, which is linked to a number of diseases from Alzheimer’s to diabetes [17–19]. Multiple studies suggest that amyloid fibril structures are a generic structure accessible to all peptide chains, regardless of sequence specificity [20–24], and can be explained by the fact that backbone intermolecular bonds stabilize these structures and hence materials. This suggests that multiple bioinspired materials of varying physico-mechanical properties can be designed. Many amphipathic peptides like hydrophobins can self-assemble at air–water/oil–water or more generally hydrophobic–hydrophilic interfaces, changing their physical and mechanical properties like surface tension [25–27]. Thus, these peptides can be exploited in tissue engineering and surface design. Fibrillar systems of β-sheets can also form hydrogels [28], which have larger applications in drug delivery and tissue regeneration therapies [29], biosensors and microfluidic design [30], and scaffolds for tissue engineering [31].
Application of Nanobioformulations for Controlled Release and Targeted Biodistribution of Drugs
Published in Anil K. Sharma, Raj K. Keservani, Rajesh K. Kesharwani, Nanobiomaterials, 2018
Josef Jampílek, Katarina Král’ová
Valo et al. (2011) employed an engineered hydrophobin fusion protein, where hydrophobin was coupled with 2 CLS binding domains in order to facilitate drug NP binding to nanofibrillar CLS. Hydrophobins are a group of small cysteine-rich proteins expressed only by filamentous fungi. Enclosing the functionalized protein coated itraconazole NPs to the external nanofibrillar CLS matrix notably increased their shelf life stability, and as a consequence of the formation of immobilized nanodispersion, dissolution rate of itraconazole was increased significantly, which also enhanced the in vivo performance of the drug.
A new hydrophobin candidate from Cladosporium macrocarpum with super-hydrophobic surface
Published in Preparative Biochemistry & Biotechnology, 2023
Büşra Albayrak Turgut, Serkan Örtücü
Hydrophobins are small, amphipathic, and surface-active proteins produced in filamentous fungi.[1] They have characteristically 8 cysteine residues which form 4 disulfide bridges (C1–C6, C2–C5, C3–C4, C7–C8) each other[2] Although hydrophobins have little similarity in amino acid sequence except having eight cysteine residues they show similar hydrophobicity.[3] Due to their self-assembly and amphipathic properties, they can form rodlet structures at the hydrophilic-hydrophobic interface; for instance, they self-assemble at air-water, water-oil, water-hydrophobic solid interface.[4,5] Based on solubility, rodlet structure they form, hydropathy pattern and also spacing between cysteine residues, they are divided into two classes, class I and II[6–9] Class I hydrophobins are soluble in TFA and formic acid, and also form rodlet structure[9,10] On the contrary of class I, class II hydrophobins are soluble in some organic solvents (e.g., 60% ethanol and acetonitrile) and 2% SDS solution and can’t form amyloid-like structures.[5]
Surfactants of microbial origin as antibiofilm agents
Published in International Journal of Environmental Health Research, 2021
Katarzyna Paraszkiewicz, Magdalena Moryl, Grażyna Płaza, Diksha Bhagat, Surekha K. Satpute, Przemysław Bernat
Both yeast and filamentous fungi can also form biofilms; however, studies of fungal biofilms are limited compared to those of yeasts (Fanning and Mitchell 2012; Cavalheiro and Teixeira 2018). Regarding yeasts, Candida albicans is the most studied model of biofilm formation and shows similar development process to those of bacterial biofilms. Sardi et al. (2015) characterized the biofilm formed by Paracoccidioides brasiliensis and found that the formation of biofilm was associated with the gene expression of adhesins and enzymes like GP43, GAPDH, and aspartyl proteinase. In recent years, studies on fungal biofilms have increased considerably. For example, in the review of Costa-Orlandi et al. (2017) the biofilm formation by filamentous fungi and some aspects of methodologies are described. The models of biofilm development in filamentous fungi – dermatophytes (Trichophytum rubrum and T. mentarophytes) and C. albicans are compared by the authors. The authors proposed a model for biofilm formation by filamentous fungi. The six stages in development of fungal biofilm are propsed: (1) propagule adsorption – contact of spores, hyphal fragments or sporangia to a surface, (2) active adhesion – adhesins are secreted by spores, (3) microcolony formation – elongation and hyphal branching, a monolayer is formed with the production of extracellular matrix, (4) second microcolony formation or initial maturation – hyphae networks form covered by an extracellular matrix and pores or channels are formed, (5) final maturation- fruiting bodies and others survivor structures are formed, (6) dispersion or planktonic phase – conidia and/or hyphae fragments are released, and a new cycle is beginning. Some filamentous fungi produce small proteins known as hydrophobins. The proteins are involved in the adhesion of hyphae and can be involved in biofilm formation.