New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities

Pimentel‐Elardo, Sheila Marie; Buback, Verena; Gulder, Tobias A. M.; Bugni, Tim S.; Reppart, Jason; Bringmann, Gerhard; Ireland, Chris M.; Schirmeister, Tanja; Hentschel, Ute

doi:10.3390/md9101682

Cited by 26 publications

(15 citation statements)

References 18 publications

(18 reference statements)

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“…In addition, these crude extracts showed immunomodulatory activity via induction of cytokine release by human peripheral blood mononuclear cells [85]. In another study, teromycins extracted from Streptomyces axinellae associated with sponge Axinellae polypoides also inhibited various proteases such as rhodesain, falcipain-2, cathepsin-L, cathepsin-B, SARS-CoV-PL pro [86]. Furthermore, the crude extracts from bacteria associated with other sponge species (e.g., Jasis sp., Plakortis nigra, Jasis stellifera, Xestospongia testudinaria, Aplysina aerophoba) showed protease inhibitory activity against subtilisin, thermolysin as well as proteases from Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa [87,88,89].…”

Section: Protease Inhibitors From Sponge and Spong-associated Microormentioning

confidence: 98%

Mini-Review PROTEASE INHIBITOR (PI) AND PIs FROM SPONGE-ASSOCIATED MICROORGANISMS

Hong¹,

Dat²,

Cúc³

et al. 2018

JST

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Protease inhibitors (PIs) are proteins or peptides inhibiting the activity of protease and constitute a very important mechanism for regulating protease activity. So far, PIs have been used for the study of enzyme structures and reaction mechanisms, but recently they have been used in pharmaceutical, agricultural and industrial fields. Compared to terrestrial counterparts, marine environment possesses their unique characters, therefore, they are capable of producing a wide range of novel bioactive compounds including protease inhibitors. In our review, a brief overview of protease inhibitors (e.g., classification, mechanisms, and characteristics of PIs) and protease inhibitors from marine sponges and sponge-associated microorganisms has been reviewed.

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Section: Protease Inhibitors From Sponge and Spong-associated Microormentioning

confidence: 98%

Mini-Review PROTEASE INHIBITOR (PI) AND PIs FROM SPONGE-ASSOCIATED MICROORGANISMS

Hong¹,

Dat²,

Cúc³

et al. 2018

JST

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“…There are some studies focused on discovery of protease inhibitory proteins from microorganisms associated with marine sponge; however, most of them use cultivation-dependent approaches (Wahyudi et al, 2010;Tabares et al, 2011;Pimentel-Elardo et al, 2011;Ramadan et al, 2012). With rapid development of advance sequencing technology, scientists begin discovering and mining novel natural products based on metagenomics instead of traditional cultivation.…”

Section: Purification Of Expressed Protein and Determination Of Its Pmentioning

confidence: 99%

Expression of a novel gene encoding protease inhibitor from metagenome of sponge in Vietnam

Hong¹,

Dat²,

Hoa³

et al. 2019

V J Bio

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Marine sponge is known as a “gold mine” of natural products from marine environment. Many novel bioactive compounds have been isolated from marine sponges and sponge-associated microorganisms such as antibiotics, anti-cancer compounds, protease inhibitors, etc. In this study, we selected a gene encoding protease inhibitor from metagenome of a sponge collected in Da Nang to express in Escherichia coli BL21(DE3). The gene PI-DN9 encoding protease inhibitor (1.3 kb) was cut off cloning vector pUC57/PI-DN9 containing gene PI-DN9 and inserted into expression vector pET32a(+), the recombinant vector pET32a(+)/PI-DN9 then was transformed and expressed in the E. coli strain BL21(DE3). Results showed that recombinant protein (50 kDa) was expressed successfully at 25°C, 1 mM of IPTG in 5 hours. The recombinant protein was purified using Ni-NTA affinity chromatography column. Western blot assay and bioactive assay showed good activity of the purified protein.

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“…Marine sponges are known to harbor diverse microbial communities [4][5][6] and represent a prolific source of natural products from their associated microorganisms [7][8][9][10] . Recent studies have shown that many potential protease inhibitors have been isolated from sponge-associated microorganisms [11][12][13][14] ; however, the exploration and exploitation potential PIs from microorganisms are still a big challenge because almost all microorganisms are resistant to cultivation in laboratory conditions, especially symbiotic microbes. Fortunately, new approaches (e.g., metagenomics) provide powerful tools for predicting, detecting and expressing novel bioactive genes from noncultured microorganisms [15][16][17][18][19] .…”

Section: Introductionmentioning

confidence: 99%

Expression and characterization of a new serine protease inhibitory protein in Escherichia coli

et al. 2020

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Introduction: Proteases are enzymes that catalyze the hydrolysis of peptide bonds and play an important role in almost all biological processes. However, excessive protein proteolysis can be implicated in several diseases, such as cancer, as well as cardiovascular, inflammatory, neurodegenerative, bacterial, viral and parasitic diseases. In these cases, protease inhibitors can be used as one of versatile tools for regulating proteolytic activity of target proteases as well as therapeutic applications. In this study, we expressed and characterized a new serine protease inhibitory protein (PI-QT) from the metagenome of sponge-associated microorganisms in Escherichia coli. Methods: The gene PI-QT encoding for a new serine protease inhibitory protein was expressed in E. coli BL21(DE3). In addition, the expressed protein was purified and characterized. Results: Optimization of expression of the recombinant protein PI-QT in E. coli showed that suitable conditions for expression of the protein were pre-induction cell density (OD600) of 0.6 - 0.7, IPTG concentration of 1 mM and temperature of 25oC. The protease inhibitory protein was also purified and identified by mass spectrometry LC-MS/MS. The recombinant protein showed inhibitory activity against trypsin anda-chymotrypsin with activity values of 97526 U/mg and 41714 U/mg, respectively. Maximum activity of the protease inhibitory protein was obtained at pH 7 and temperature 20-35oC. The inhibitor was stable over pH 4-9 and up to temperature 50oC. Addition of Zn2+, Mg2+ and Ca2+ enhanced inhibitory activity, whereas other metal ions, surfactants and oxidants reduced inhibitory activity of the protease inhibitor. Conclusion: The recombinant protein PI-QT is a potential protease inhibitor for therapeutic applications.

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New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities

Cited by 26 publications

References 18 publications

Mini-Review PROTEASE INHIBITOR (PI) AND PIs FROM SPONGE-ASSOCIATED MICROORGANISMS

Mini-Review PROTEASE INHIBITOR (PI) AND PIs FROM SPONGE-ASSOCIATED MICROORGANISMS

Expression of a novel gene encoding protease inhibitor from metagenome of sponge in Vietnam

Expression and characterization of a new serine protease inhibitory protein in Escherichia coli

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