A hydrophobic segment of some cytotoxic ribonucleases

Ширшиков, Ф. В.; Черепнев, Г. В.; Ilinskaya, О. N.; Kalacheva, N. V.

doi:10.1016/j.mehy.2013.04.006

Cited by 10 publications

(11 citation statements)

References 43 publications

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“…Existence of two molecular forms of binase, a monomeric and a dimeric one, was considered by Polyakov et al [34], Konovalova et al [35], Shirshikov et al [36], and Ermakova [37]. In these works, how ever, existence of dimeric structures formed due to hydrogen bonds and hydrophobic interactions was theoretically proposed in binase crystals, while their formation in solutions was considered hypothetical [34,36].…”

Section: Resultsmentioning

confidence: 99%

“…In these works, how ever, existence of dimeric structures formed due to hydrogen bonds and hydrophobic interactions was theoretically proposed in binase crystals, while their formation in solutions was considered hypothetical [34,36]. Formation of dimeric and aggregated forms of binase on the membrane surface, which may enhance the penetration of this enzyme into the cell, is also probable [35].…”

Section: Resultsmentioning

confidence: 99%

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Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

et al. 2015

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Immunochemical analysis of the following purified preparations of Bacillus pumilus RNase (binase) was carried out: industrially manufactured enzyme (Institute of Organic Synthesis, Riga, Latvia) and the enzymes isolated from the culture liquid of the native B. pumilus producer and from the Escherichia coli BL21 recombinant strain bearing the pGEMGX1/ent/Bi plasmid. Electrophoresis of all three samples of purified binase revealed two protein fractions with ribonuclease activity possessing molecular masses of ~12 and 25 kDa. The possible presence of binase II, a second secreted RNase, was ruled out. Both high and low molecular mass proteins interacted with binase specific antibodies in the immunoblotting reaction, which indicated their antigenic identity. The difference in molecular mass between these proteins indicated the pos sible presence of two forms of binase in solution, a monomer and a dimer.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

et al. 2015

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“…The obtained experimental results are in good agreement with the theoretical ones. In previously published work 30 , we found in silico that in the molecule of binase there is a hydrophobic (NF) segment, in which structure we identified amino acid residues required for the dimerization. Thermodynamic parameters of the NFsegment show that it is capable of thermodynamically favorable interaction with the lipid bilayer and sterically available for the dimerization of monomers binase.…”

Section: Discussionmentioning

confidence: 96%

Surface-Dependent Differences in the Adsorption of Pancreatic and Microbial Ribonucleases Visualized by Atomic Force Microscopy

Коновалова¹,

Kalacheva²,

Черепнев³

et al. 2016

Biosci., Biotech. Res. Asia

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A comparative study of the physical adsorption of RNAse A and RNAse Bacillus pumilis onto a negatively charged surface of mica, a hydrophobic surface of pyrolytic graphite and a surface of lipid layers of dipalmitoylphosphatidylcholine (DPPC) was performed by atomic force microscopy. It was found that microbial RNAse, unlike RNAse A, 1) is adsorbed onto the negatively charged surface of mica in the form of monomers and dimers; 2) exhibits enhanced tropism to the hydrophobic surface of pyrolytic graphite; 3) modifies morphotopography and thickness of the lipid bilayer of DPPC. The detected surface-dependent differences in adsorption of RNAses are consistent with the features of their structure and cytotoxic properties.

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“…In addition, for RNase A, it has been described a multipathway of internalization that involves both clathrin-coated vesicles and macropinosomes [57]. Finally, through an in silico study by sliding-window hydrophobicity analysis, it has been hypothesized that some cytotoxic RNases have a hydrophobic segment sterically available for a hydrophobic interaction with both tumor cell and endosomal membranes that would facilitate their internalization [58]. The more it is known about the membrane structures that are recognized by RNases or the productive pathway, by which they enter the cell, the better they can be engineered to increase their selectivity and potency.…”

Section: What Makes a Ribonuclease Selectively Cytotoxic For Cancer Cmentioning

confidence: 99%

Approaches to Endow Ribonucleases with Antitumor Activity: Lessons Learned from the Native Cytotoxic Ribonucleases

Castro¹,

Ribó²,

Benito³

et al. 2016

Anti-Cancer Drugs - Nature, Synthesis and Cell

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Typical antitumor drugs disrupt the flow of biochemical information from DNA to proteins with the aim of precluding uncontrolled cell proliferation and inducing cancer cell apoptosis. However, most of the currently used small antitumor drugs are genotoxic because they act over DNA. Pharmaceutical industry is now searching for a new line of cancer chemotherapeutics without genotoxic effects. Ribonucleases (RNases) are small basic proteins, present in all life forms, which belong to this kind of chemotherapeutics. Some of them present with remarkable selective antitumor activity linked to their ability to destroy RNA, a powerful way to control gene expression, leaving DNA unharmed. In the last two decades, the knowledge gained on the cytotoxic mechanism of these RNases has been used to engineer more powerful and selective variants to kill cancer cells. In this chapter, we describe the advances reached in endowing an RNase with antitumor abilities.

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A hydrophobic segment of some cytotoxic ribonucleases

Cited by 10 publications

References 43 publications

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

Surface-Dependent Differences in the Adsorption of Pancreatic and Microbial Ribonucleases Visualized by Atomic Force Microscopy

Approaches to Endow Ribonucleases with Antitumor Activity: Lessons Learned from the Native Cytotoxic Ribonucleases

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