Self‐assembly of two hydrophobins from marine fungi affected by interaction with surfaces

Abstract

Hydrophobins are amphiphilic fungal proteins endowed with peculiar characteristics, such as a high surface activity and an interface triggered self-assembly. Several applications of these proteins have been proposed in the food, cosmetics and biomedical fields. Moreover, their use as proteinaceous coatings can be effective for materials and nanomaterials applications. The discovery of novel hydrophobins with diverse properties may be advantageous from both the scientific and industrial points of view. Stressful environmental conditions of fungal growth may induce the production of proteins with peculiar features. Two Class I hydrophobins from fungi isolated from marine environment have been recently purified. Herein, their propensity to aggregate forming nanometric fibrillar structures has been compared, using different techniques, such as circular dichroism, dynamic light scattering and Thioflavin T fluorescence assay. Furthermore, TEM and AFM images indicate that the interaction of these proteins with specific surfaces, are crucial in the formation of amyloid fibrils and in the assembly morphologies. These self-assembling proteins show promising properties as bio-coating for different materials via a green process. Biotechnol. Bioeng. 2017;114: 2173-2186. © 2017 Wiley Periodicals, Inc.

Cerato-Platanins from Marine Fungi as Effective Protein Biosurfactants and Bioemulsifiers

“…As far as the comparison of CPs with HFBs is concerned, it was reported that some CPs form amyloid-like aggregates, but only under stress conditions [26,27]. In fact, ThCP and AtCP do not show the same propensity to form amyloid-like fibrils as Class I HFBs, since the CD spectra of ThCP and AtCP were unchanged even after one month, differently from what occurs to Class I HFBs, which change their conformation after some days in mild conditions [28,29].…”

The Protean Acremonium. A. sclerotigenum/egyptiacum: Revision, Food Contaminant, and Human Disease

“…Other industrial explorations have shown that the species can affect some potentially useful transformations of pharmaceutically produced steroids [ 43 ]. A recent study has stated that an A. egyptiacum (identified as A. sclerotigenum ) isolate obtained from Flabellia petiolata marine alga produces amyloidogenic hydrophobin proteins that may be of interest in the manufacture of ‘green’ bio-coatings [ 44 ]. However, a search in GenBank for sequences from this study yielded only accession KR014351 for strain MUT-4872; this sequence matches a known undescribed species related to Acremonium hennebertii .…”

<i>In vivo</i> Bioengineering of Fluorescent Conductive Protein-Dye Microfibers

“…The sample preparation followed the procedure previously reported. (Cicatiello et al, 2017) , (Oliviero et al, 2017) Briefly, 5 mL aliquots of the sample/imaging buffer were directly deposited by casting onto the substrate; after 2 min, samples were gently washed with deionized water in order to remove cell and salt traces, then, dried by evaporation at room temperature under a ventilated fume hood. Fluorescent fibrils were individuated by means of fluorescence microscopy (Leica Z16 APO fluorescence microscope equipped with a Leica camera DFC320; filter sets: 450-490 nm band-pass excitation filter, a 510 nm dichromatic mirror and a 515 nm suppression filter) and then the same imaging field was analysed by AFM and EFM.…”