scholarly journals Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology

Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 6785
Author(s):  
Olga Shilova ◽  
Polina Kotelnikova ◽  
Galina Proshkina ◽  
Elena Shramova ◽  
Sergey Deyev
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
High Stability ◽  
Suicide Gene ◽  
Anticancer Therapy ◽  
Supramolecular Complexes ◽  
High Solubility ◽  
Anticancer Compounds ◽  
Protein Protein Interaction ◽  
Experimental Cancer ◽  
Self Aggregation

Barnase is an extracellular ribonuclease secreted by Bacillus amyloliquefaciens that was originally studied as a small stable enzyme with robust folding. The identification of barnase intracellular inhibitor barstar led to the discovery of an incredibly strong protein-protein interaction. Together, barnase and barstar provide a fully genetically encoded toxin-antitoxin pair having an extremely low dissociation constant. Moreover, compared to other dimerization systems, the barnase-barstar module provides the exact one-to-one ratio of the complex components and possesses high stability of each component in a complex and high solubility in aqueous solutions without self-aggregation. The unique properties of barnase and barstar allow the application of this pair for the engineering of different variants of targeted anticancer compounds and cytotoxic supramolecular complexes. Using barnase in suicide gene therapy has also found its niche in anticancer therapy. The application of barnase and barstar in contemporary experimental cancer therapy is reflected in the review.

scholarly journals Phase Behavior and DFT Calculations of Laterally Methyl Supramolecular Hydrogen-Bonding Complexes

Crystals ◽  
2019 ◽  
Vol 9 (3) ◽  
pp. 133 ◽  
Author(s):  
Hoda Ahmed ◽  
Mohamed Hagar ◽  
Omaima Alhaddad
Keyword(s):  
Differential Scanning Calorimetry ◽  
High Stability ◽  
Polarized Light ◽  
Supramolecular Complexes ◽  
Scanning Calorimetry ◽  
Methyl Group ◽  
Smectic C ◽  
Computational Calculations ◽  
Nematic Phases ◽  
Hydrogen Bonded

Four new series of laterally methyl-substituted hydrogen-bonded supramolecular complexes were prepared. The prepared complexes were thermally investigated by differential scanning calorimetry (DSC) and phases identified by polarized light microscopy (PLM). Supramolecular hydrogen-bonded complexes formed from a 1:1 mixture of any two derivatives, bearing different alkoxy chains, of 4-alkoxyphenylazobenzoic acid and 4-(2-(pyridin-4-yl)diazenyl-(2-(or 3-)methylphenyl) 4-alkoxybenzoate. The investigated 1:1 mixture made by introducing a lateral methyl group by different spatial orientation angles into pyridine-based components. All new complexes were confirmed by Fourier-transform infrared spectroscopy (FTIR) and computational calculations used to study their stabilities. It is found that the prepared complexes are dimorphic, exhibiting smectic C and enhanced nematic phases. A comparison was made between the new series and previously investigated simpler complexes, revealed that the incorporation of the phenylazo group elongate the mesogenic part and hence broad nematic phases were obtained with high stability.

scholarly journals Phenotype and target-based chemical biology investigations in cancers

2018 ◽  
Vol 6 (6) ◽  
pp. 1111-1127 ◽  
Author(s):  
Guo-Qiang Chen ◽  
Ying Xu ◽  
Shao-Ming Shen ◽  
Jian Zhang
Keyword(s):  
Protein Interactions ◽  
Cancer Biology ◽  
Chemical Biology ◽  
Molecular Mechanisms ◽  
Target Identification ◽  
Expression System ◽  
Protein Protein Interactions ◽  
Anticancer Compounds ◽  
Protein Protein Interaction ◽  
Mechanisms Of Carcinogenesis

Abstract Chemical biology has been attracting a lot of attention because of the key roles of chemical methods and techniques in helping to decipher and manipulate biological systems. Although chemical biology encompasses a broad field, this review will focus on chemical biology aimed at using exogenous chemical probes to interrogate, modify and manipulate biological processes, at the cellular and organismal levels, in a highly controlled and dynamic manner. In this area, many advances have been achieved for cancer biology and therapeutics, from target identification and validation based on active anticancer compounds (forward approaches) to discoveries of anticancer molecules based on some important targets including protein-protein interaction (reverse approaches). Herein we attempt to summarize some recent progresses mainly from China through applying chemical biology approaches to explore molecular mechanisms of carcinogenesis. Additionally, we also outline several new strategies for chemistry to probe cellular activities such as proximity-dependent labeling methods for identifying protein-protein interactions, genetically encoded sensors, and light activating or repressing gene expression system.

scholarly journals Isolation of Cell-Free miRNA from Biological Fluids: Influencing Factors and Methods

Diagnostics ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 865
Author(s):  
Olga Bryzgunova ◽  
Maria Konoshenko ◽  
Ivan Zaporozhchenko ◽  
Alexey Yakovlev ◽  
Pavel Laktionov
Keyword(s):  
Clinical Research ◽  
Structural Properties ◽  
Influencing Factors ◽  
High Stability ◽  
Biological Fluids ◽  
Supramolecular Complexes ◽  
Clinical Settings ◽  
Downstream Analysis ◽  
Extracellular Environment

A vast wealth of recent research has seen attempts of using microRNA (miRNA) found in biological fluids in clinical research and medicine. One of the reasons behind this trend is the apparent their high stability of cell-free miRNA conferred by small size and packaging in supramolecular complexes. However, researchers in both basic and clinical settings often face the problem of selecting adequate methods to extract appropriate quality miRNA preparations for use in specific downstream analysis pipelines. This review outlines the variety of different methods of miRNA isolation from biofluids and examines the key determinants of their efficiency, including, but not limited to, the structural properties of miRNA and factors defining their stability in the extracellular environment.

Anticancer Polyphenols from Cultured Plant Cells: Production and New Bioengineering Strategies

2018 ◽  
Vol 25 (36) ◽  
pp. 4671-4692 ◽  
Author(s):  
V.P. Bulgakov ◽  
Y.V. Vereshchagina ◽  
G.N. Veremeichik
Keyword(s):  
Phenolic Acids ◽  
Plant Cells ◽  
Main Trend ◽  
Cancer Cell Proliferation ◽  
Anticancer Compounds ◽  
Gene Effects ◽  
Protein Protein Interaction ◽  
Comprehensive Knowledge ◽  
Prevention Of Cancer ◽  
Prevent Tumor Growth

Background: For many years, anticancer polyphenols have attracted significant attention as substances that prevent tumor growth and progression. These compounds are simple phenolic acids, complex phenolic acids, such as caffeoylquinic acids, rosmarinic acid and its derivatives, stilbenes, flavones, isoflavones, and anthocyanins. Some compounds, such as tea and coffee polyphenols, can be produced in large quantities by traditional methods, while many others cannot. <p> Methods: We reviewed the available literature regarding the biotechnological aspects of polyphenol production by cultured plant cells and described approaches that have been used to obtain high levels of anticancer polyphenols (resveratrol, podophyllotoxin, genistein, lithospermic acid B, and others). Additionally, we provide our view on bioengineering strategies that could be important for the further improvement of cell biosynthetic characteristics. <p> Results: The main trend in the field is the activation of entire biosynthetic pathways based on a comprehensive knowledge of protein-protein interaction networks involved in the regulation of polyphenol biosynthesis. As an example, we consider the jasmonate subnetwork, which will be increasingly used by plant biotechnologists. The next-generation technologies to sustained polyphenol production involve manipulations with microRNAs and reproduction of rol-gene effects. <p> Conclusion: Plant polyphenols play an important role in maintaining human health, and their role in the prevention of cancer will continue to grow. Targeting mechanisms involved in uncontrolled cancer cell proliferation will increasingly become the standard for cancer patients. Plant biotechnological studies aiming at producing anticancer compounds will be developed in parallel with these studies to provide a wider range of metabolites for each particular case.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

POPDC proteins and cardiac function

2019 ◽  
Vol 47 (5) ◽  
pp. 1393-1404 ◽  
Author(s):  
Thomas Brand
Keyword(s):  
Potential Role ◽  
Striated Muscle ◽  
Short Review ◽  
Effector Proteins ◽  
Muscle Disease ◽  
Disease Genes ◽  
Protein Protein Interaction ◽  
Interaction Partners ◽  
And Function

Abstract The Popeye domain-containing gene family encodes a novel class of cAMP effector proteins in striated muscle tissue. In this short review, we first introduce the protein family and discuss their structure and function with an emphasis on their role in cyclic AMP signalling. Another focus of this review is the recently discovered role of POPDC genes as striated muscle disease genes, which have been associated with cardiac arrhythmia and muscular dystrophy. The pathological phenotypes observed in patients will be compared with phenotypes present in null and knockin mutations in zebrafish and mouse. A number of protein–protein interaction partners have been discovered and the potential role of POPDC proteins to control the subcellular localization and function of these interacting proteins will be discussed. Finally, we outline several areas, where research is urgently needed.

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