Characterization of a Surface-Active Protein Extracted from a Marine Strain of Penicillium chrysogenum

Cicatiello, Paola; Stanzione, Ilaria; Dardano, Principia; Stefano, Luca De; Birolo, Leila; Chiaro, Addolorata De; Monti, Daria Maria; Petruk, Ganna; D’Errico, Gerardino; Giardina, Paola

doi:10.3390/ijms20133242

Cited by 17 publications

(11 citation statements)

References 37 publications

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“…Therefore, as a first approach, the ability of both proteins to stabilize emulsions was verified. Indeed, the obtained E 24 values were comparable to those of other proteins and to commercially available surfactants analyzed in the same way [19,23].…”

Section: Discussionsupporting

confidence: 76%

“…We also analyzed the surface tension reduction of these CPs and unexpectedly observed that ThCP behaves as a good BS, beyond being a good BE. Indeed, the surface tension value reached in the presence of ThCP was much lower than those of AtCP and of Sap-Pc, another BE protein recently purified from a marine strain of Penicillium chrysogenum, measured in comparable conditions [23].…”

Section: Discussionmentioning

confidence: 92%

“…Because these proteins are poorly stained with Coomassie Brilliant Blue, the samples were loaded in duplicates on the same gel and a set of samples was Coomassie stained, whereas the other set was analyzed by silver staining. By superimposing the Coomassie-stained and silver-stained protein bands, we localized the protein bands corresponding to the proteins of interest (apparent molecular mass between 12 and 17 kDa), which were excised from gel and processed as reported in Cicatiello et al [23] on a 6520 Accurate-Mass Q-TOF LC/MS system (Agilent Technologies, Palo Alto, CA, USA) equipped with a 1200 HPLC system and a chip cube. The acquired MS/MS spectra were transformed in Mascot Generic Format (.mgf) and used to query the NCBI nonredundant (NR) database (http://www.ncbi.nlm.nih.gov), version 20160114, 79 354 501 sequences and 28 992 349 963 residues for "Fungi" as taxonomy restriction, for protein identification with a licensed version of MASCOT software (www.matrixscience.com) version 2.4.0, which was performed as previously described [25].…”

Section: Protein Identification By Mass Spectrometrymentioning

confidence: 99%

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

Pitocchi

Cicatiello

Birolo

et al. 2020

IJMS

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Two fungal strains, Aspergillus terreus MUT 271 and Trichoderma harzianum MUT 290, isolated from a Mediterranean marine site chronically pervaded by oil spills, can use crude oil as sole carbon source. Herein, these strains were investigated as producers of biosurfactants, apt to solubilize organic molecules as a preliminary step to metabolize them. Both fungi secreted low molecular weight proteins identified as cerato-platanins, small, conserved, hydrophobic proteins, included among the fungal surface-active proteins. Both proteins were able to stabilize emulsions, and their capacity was comparable to that of other biosurfactant proteins and to commercially available surfactants. Moreover, the cerato-platanin from T. harzianum was able to lower the surface tension value to a larger extent than the similar protein from A. terreus and other amphiphilic proteins from fungi. Both cerato-platanins were able to make hydrophilic a hydrophobic surface, such as hydrophobins, and to form a stable layer, not removable even after surface washing. To the best of our knowledge, the ability of cerato-platanins to work both as biosurfactant and bioemulsifier is herein demonstrated for the first time.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 92%

Section: Protein Identification By Mass Spectrometrymentioning

confidence: 99%

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

Pitocchi

Cicatiello

Birolo

et al. 2020

IJMS

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“…A comparable two‐stage decrease in surface tension was observed in the surface‐active Sap‐Pc protein from a marine strain of Penicillium chrysogenum . [ 28 ] Altogether these results indicate for the first time, at least to our knowledge, that the p‐gliadin is composed of self‐associated peptides that are active at the water/air interface. These C.A.C values are much below than the 1 mg mL −1 usually employed in biomedical research, which implies that large p‐gliadin supramolecular structures should be present in vitro studies.…”

Section: Resultsmentioning

confidence: 65%

Pepsin Digest of Gliadin Forms Spontaneously Amyloid‐Like Nanostructures Influencing the Expression of Selected Pro‐Inflammatory, Chemoattractant, and Apoptotic Genes in Caco‐2 Cells: Implications for Gluten‐Related Disorders

Herrera

Nicoletti

Gras

et al. 2021

Molecular Nutrition Food Res

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Scope Proteolysis‐resistant gliadin peptides are intensely investigated in biomedical research relates to celiac disease and gluten‐related disorders. Herein, the first integrated supramolecular investigation of pepsin‐digested gliadin peptides (p‐gliadin) is presented in combination with its functional behavior in the Caco‐2 cell line. Methods and Results First, gliadins are degraded by pepsin at pH 3, and the physicochemical properties of p‐gliadin are compared with gliadin. An integrated approach using interfacial, spectroscopic, and microscopic techniques reveals that the p‐gliadin forms spontaneously soluble large supramolecular structures, mainly oligomers and fibrils, capable of binding amyloid‐sensitive dyes. The self‐assembly of p‐gliadin starts at a concentration of 0.40 µg mL−1. Second, the stimulation of Caco‐2 cells with the p‐gliadin supramolecular system is performed, and the mRNA expression levels of a panel of genes are tested. The experiments show that p‐gliadin composed of supramolecular structures triggers significant mRNA up‐regulation (p < 0.05) of pro‐apoptotic biomarkers (ratio Bcl2/Bak‐1), chemokines (CCL2, CCL3, CCL4, CCL5, CXCL8), and the chemokine receptor CXCR3. Conclusions This work demonstrates that p‐gliadin is interfacial active, forming spontaneously amyloid‐type structures that trigger genes in the Caco‐2 cell line involved in recruiting specialized immune cells.

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“…Marine proteins are mainly isolated from marine organisms such as sponges [8], sea squirts [9], mollusks [10], algae [11], marine fungi [12], and marine strain [13]. A large number of investigations have shown that marine proteins exert good antitumor effects.…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a Novel Protein ASP-3 Purified from Arca subcrenata and Its Antitumor Mechanism

Guo

Shi

et al. 2019

Marine Drugs

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Diverse bioactive substances derived from marine organisms have been attracting growing attention. Besides small molecules and polypeptides, numerous studies have shown that marine proteins also exhibit antitumor activities. Small anticancer proteins can be expressed in vivo by viral vectors to exert local and long-term anticancer effects. Herein, we purified and characterized a novel protein (ASP-3) with unique antitumor activity from Arca subcrenata Lischke. The ASP-3 contains 179 amino acids with a molecular weight of 20.6 kDa. The spectral characterization of ASP-3 was elucidated using Fourier Transform infrared spectroscopy (FTIR) and Circular Dichroism (CD) spectroscopy. Being identified as a sarcoplasmic calcium-binding protein, ASP-3 exhibited strong inhibitory effects on the proliferation of Human hepatocellular carcinoma (HepG2) cells with an IC50 value of 171.18 ± 18.59 μg/mL, measured by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. The RNA-seq analysis showed that ASP-3 regulated the vascular endothelial growth factor receptor (VEGFR) signaling pathway in HepG2 cells. Immunofluorescence results indicated that ASP-3 effectively reduced VEGFR2 phosphorylation in HepG2 cells and affected the downstream components of VEGF signaling pathways. The surface plasmon resonance (SPR) analysis further demonstrated that ASP-3 direct interacted with VEGFR2. More importantly, the therapeutic potential of ASP-3 as an anti-angiogenesis agent was further confirmed by an in vitro model using VEGF-induced tube formation assay of human umbilical vein endothelial cells (HUVECs), as well as an in vivo model using transgenic zebrafish model. Taken together, the ASP-3 provides a good framework for the development of even more potent anticancer proteins and provides important weapon for cancer treatment using novel approaches such as gene therapy.

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Characterization of a Surface-Active Protein Extracted from a Marine Strain of Penicillium chrysogenum

Cited by 17 publications

References 37 publications

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

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

Pepsin Digest of Gliadin Forms Spontaneously Amyloid‐Like Nanostructures Influencing the Expression of Selected Pro‐Inflammatory, Chemoattractant, and Apoptotic Genes in Caco‐2 Cells: Implications for Gluten‐Related Disorders

Identification and Characterization of a Novel Protein ASP-3 Purified from Arca subcrenata and Its Antitumor Mechanism

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