Relevant bibliographies by topics / Azurin protein

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Academic literature on the topic 'Azurin protein'

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Published: 6 September 2023

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Journal articles on the topic "Azurin protein"

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Yamada, Tohru, Masatoshi Goto, Vasu Punj, Olga Zaborina, Kazuhide Kimbara, T. K. Das Gupta, and A. M. Chakrabarty. "The Bacterial Redox Protein Azurin Induces Apoptosis in J774 Macrophages through Complex Formation and Stabilization of the Tumor Suppressor Protein p53." Infection and Immunity 70, no. 12 (December 2002): 7054–62. http://dx.doi.org/10.1128/iai.70.12.7054-7062.2002.

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ABSTRACT Two redox proteins, azurin and cytochrome c 551 elaborated by Pseudomonas aeruginosa, demonstrate significant cytotoxic activity towards macrophages. Azurin can enter macrophages, localize in the cytosol and nuclear fractions, and induce apoptosis. Two redox-negative mutants of azurin have less cytotoxicity than does wild-type (wt) azurin. Azurin has been shown to form a complex with the tumor suppressor protein p53, a known inducer of apoptosis, thereby stabilizing it and enhancing its intracellular level. A higher level of reactive oxygen species (ROS), generated during treatment of macrophages with wt azurin, correlates with its cytotoxicity. Treatment with some ROS-removing antioxidants greatly reduces azurin-mediated cytotoxicity, thus demonstrating a novel virulence property of this bacterial redox protein.
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Aslam, Shakira, Hafiz Muzzammel Rehman, Muhammad Zeeshan Sarwar, Ajaz Ahmad, Nadeem Ahmed, Muhammad Imran Amirzada, Hafiz Muhammad Rehman, Humaira Yasmin, Tariq Nadeem, and Hamid Bashir. "Computational Modeling, High-Level Soluble Expression and In Vitro Cytotoxicity Assessment of Recombinant Pseudomonas aeruginosa Azurin: A Promising Anti-Cancer Therapeutic Candidate." Pharmaceutics 15, no. 7 (June 26, 2023): 1825. http://dx.doi.org/10.3390/pharmaceutics15071825.

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Azurin is a natural protein produced by Pseudomonas aeruginosa that exhibits potential anti-tumor, anti-HIV, and anti-parasitic properties. The current study aimed to investigate the potential of azurin protein against breast cancer using both in silico and in vitro analyses. The amino acid sequence of Azurin was used to predict its secondary and tertiary structures, along with its physicochemical properties, using online software. The resulting structure was validated and confirmed using Ramachandran plots and ERRAT2. The mature azurin protein comprises 128 amino acids, and the top-ranked structure obtained from I-TASSER was shown to have a molecular weight of 14 kDa and a quality factor of 100% by ERRAT2, with 87.4% of residues in the favored region of the Ramachandran plot. Docking and simulation studies of azurin protein were conducted using HDOCK and Desmond servers, respectively. The resulting analysis revealed that Azurin docked against p53 and EphB2 receptors demonstrated maximum binding affinity, indicating its potential to cause apoptosis. The recombinant azurin gene was successfully cloned and expressed in a BL21 (DE3) strain using a pET20b expression vector under the control of the pelB ladder, followed by IPTG induction. The azurin protein was purified to high levels using affinity chromatography, yielding 70 mg/L. In vitro cytotoxicity assay was performed using MCF-7 cells, revealing the significant cytotoxicity of the azurin protein to be 105 µg/mL. These findings highlight the potential of azurin protein as an anticancer drug candidate.
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Valli S, Abiraami, and Mythili T. "BIOINFORMATIC STUDY OF AN ANTITUMOR PROTEIN, AZURIN." Asian Journal of Pharmaceutical and Clinical Research 11, no. 6 (June 7, 2018): 169. http://dx.doi.org/10.22159/ajpcr.2018.v11i6.23339.

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Objective: The main objective of this study is to analyze the structure and function of an antitumor protein, azurin, thereby giving validation to the protein structure and existing physicochemical properties in the anticancer protein which are responsible for the anticancer activity.Methods: Protein sequence analysis was done using Basic Local Alignment Search Tool (BLAST) with ten different randomly selected species of Pseudomonas obtained from GenBank. The physicochemical properties, prediction of secondary structure, identification of motifs and domains, three-dimensional (3-D) structure of the antitumor protein, validation through Ramachandran plot, multiple sequence alignment (MSA), and phylogenetic analysis were studied and functional property was confirmed through in silico docking.Results: The similarity search (BLAST-P analysis) for the primary sequence from GenBank carried out showed 86% similarity to the second sequence, azurin (Pseudomonas nitroreducens). The ProtParam, ExPASy tool server indicated the presence of essential physicochemical properties in azurin. Secondary structure prediction revealed random coil, extended strand, alpha helix, and beta turn. The study on domains indicated the presence of one domain in azurin responsible for the anticancer activity. The 3-D structural analysis revealed azurin as metalloprotein, of length-128, and polymer-1 with α-helices, β-sheets, and β-barrels. The validation carried out through Ramachandran plot showed the presence of two outliers (phi and psi). The biological relationship between the input sequences was studied through MSA and phylogenetic analysis. Further, azurin docked against the target protein (p53 tumor suppressor) showed the maximum binding affinity confirming its functional property of causing apoptosis.Conclusion: All the properties analyzed in the present study revealed that the azurin protein can act as a very good anticancer agent, and through the phylogenetic analysis, it was identified that Pseudomonas nitroreducens was closely related to the test organism Pseudomonas aeruginosa.
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Signorelli, Sara, Salvatore Cannistraro, and Anna Rita Bizzarri. "Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin." International Journal of Molecular Sciences 20, no. 12 (June 24, 2019): 3078. http://dx.doi.org/10.3390/ijms20123078.

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Raman spectroscopy, which is a suitable tool to elucidate the structural properties of intrinsically disordered proteins, was applied to investigate the changes in both the structure and the conformational heterogeneity of the DNA-binding domain (DBD) belonging to the intrinsically disordered protein p53 upon its binding to Azurin, an electron-transfer anticancer protein from Pseudomonas aeruginosa. The Raman spectra of the DBD and Azurin, isolated in solution or forming a complex, were analyzed by a combined analysis based on peak inspection, band convolution, and principal component analysis (PCA). In particular, our attention was focused on the Raman peaks of Tyrosine and Tryptophan residues, which are diagnostic markers of protein side chain environment, and on the Amide I band, of which the deconvolution allows us to extract information about α-helix, β-sheet, and random coil contents. The results show an increase of the secondary structure content of DBD concomitantly with a decrease of its conformational heterogeneity upon its binding to Azurin. These findings suggest an Azurin-induced conformational change of DBD structure with possible implications for p53 functionality.
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Naguleswaran, Arunasalam, Arsenio M. Fialho, Anita Chaudhari, Chang Soo Hong, Ananda M. Chakrabarty, and William J. Sullivan. "Azurin-Like Protein Blocks Invasion of Toxoplasma gondii through Potential Interactions with Parasite Surface Antigen SAG1." Antimicrobial Agents and Chemotherapy 52, no. 2 (December 10, 2007): 402–8. http://dx.doi.org/10.1128/aac.01005-07.

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ABSTRACT Some pathogenic bacteria produce factors that have evolved a capacity to neutralize competing microbes. The cupredoxin family protein azurin, produced by Pseudomonas aeruginosa, exhibits a remarkable ability to impede invasion of a number of diverse intracellular pathogens, including the human AIDS virus human immunodeficiency virus type 1 and the protozoan parasite Plasmodium falciparum (which causes malaria). Here we report that azurin and an azurin-like protein (Laz) from gonococci/meningococci have activity against Toxoplasma, an apicomplexan parasite that causes opportunistic infection in immunocompromised individuals. We demonstrate that the mechanism of action for Laz involves interfering with the ability of Toxoplasma to adhere to host cells. Computer structural analysis reveals that azurin shares structural features with the predominant surface antigen SAG1, which is known to play an important role in parasite attachment. Interestingly, azurin also has structural similarities to a monoclonal antibody to SAG1. Surface plasmon resonance binding studies validate that SAG1 interacts strongly with Laz and, to lesser extent, azurin. Moreover, Toxoplasma mutants lacking SAG1 are not as susceptible to the growth-inhibitory effects of Laz. Collectively, our data show that Toxoplasma adhesion can be significantly impaired by Laz, and to some extent by azurin, via interactions with SAG1. These observations indicate that Laz can serve as an important tool in the study of host-pathogen interactions and is worthy of further study for development into potential therapeutic agents.
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Gammuto, Leandro, Carolina Chiellini, Marta Iozzo, Renato Fani, and Giulio Petroni. "The Azurin Coding Gene: Origin and Phylogenetic Distribution." Microorganisms 10, no. 1 (December 22, 2021): 9. http://dx.doi.org/10.3390/microorganisms10010009.

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Azurin is a bacterial-derived cupredoxin, which is mainly involved in electron transport reactions. Interest in azurin protein has risen in recent years due to its anticancer activity and its possible applications in anticancer therapies. Nevertheless, the attention of the scientific community only focused on the azurin protein found in Pseudomonas aeruginosa (Proteobacteria, Gammaproteobacteria). In this work, we performed the first comprehensive screening of all the bacterial genomes available in online repositories to assess azurin distribution in the three domains of life. The Azurin coding gene was not detected in the domains Archaea and Eucarya, whereas it was detected in phyla other than Proteobacteria, such as Bacteroidetes, Verrucomicrobia and Chloroflexi, and a phylogenetic analysis of the retrieved sequences was performed. Observed patchy distribution and phylogenetic data suggest that once it appeared in the bacterial domain, the azurin coding gene was lost in several bacterial phyla and/or anciently horizontally transferred between different phyla, even though a vertical inheritance appeared to be the major force driving the transmission of this gene. Interestingly, a shared conserved domain has been found among azurin members of all the investigated phyla. This domain is already known in P. aeruginosa as p28 domain and its importance for azurin anticancer activity has been widely explored. These findings may open a new and intriguing perspective in deciphering the azurin anticancer mechanisms and to develop new tools for treating cancer diseases.
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Ambler, R. P., and J. Tobari. "Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J." Biochemical Journal 261, no. 2 (July 15, 1989): 495–99. http://dx.doi.org/10.1042/bj2610495.

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Methylomonas J is an obligate methylotroph although it is unable to grow on methane. Like Pseudomonas AM1, it produces two blue copper proteins when growing on methylamine, one of which is the recipient of electrons from the methylamine dehydrogenase. When grown on methanol, only the other blue copper protein is produced. We have determined the amino acid sequences of these blue copper proteins, and show that they are both true azurins. The sequences are clearly homologous to those of the proteins characterized from fluorescent pseudomonads and various species of Alcaligenes, and can be aligned with them and with each other without the need to postulate any internal insertions or deletions in the sequences. The iso-1 azurin, the one produced during both methanol and methylamine growth, shows 59-65% identity with these other azurins, whereas the iso-2 protein shows only 47-53% identity. The proteins show 52% identity with each other. The two functionally equivalent blue copper proteins from Pseudomonas AM1 belong to two sequence classes that are quite distinct from the true azurins. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50151 (23 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257, 5.
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Fialho, Arsenio M., Prabhakar Salunkhe, Sunil Manna, Sidharth Mahali, and Ananda M. Chakrabarty. "Glioblastoma Multiforme: Novel Therapeutic Approaches." ISRN Neurology 2012 (February 8, 2012): 1–10. http://dx.doi.org/10.5402/2012/642345.

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The current therapy for glioblastoma multiforme involves total surgical resection followed by combination of radiation therapy and temozolomide. Unfortunately, the efficacy for such current therapy is limited, and newer approaches are sorely needed to treat this deadly disease. We have recently described the isolation of bacterial proteins and peptides with anticancer activity. In phase I human clinical trials, one such peptide, p28, derived from a bacterial protein azurin, showed partial and complete regression of tumors in several patients among 15 advanced-stage cancer patients with refractory metastatic tumors where the tumors were no longer responsive to current conventional drugs. An azurin-like protein called Laz derived from Neisseria meningitides demonstrates efficient entry and high cytotoxicity towards glioblastoma cells. Laz differs from azurin in having an additional 39-amino-acid peptide called an H.8 epitope, which allows entry and high cytotoxicity towards glioblastoma cells. Since p28 has been shown to have very little toxicity and high anti-tumor activity in advanced-stage cancer patients, it will be worthwhile to explore the use of H.8-p28, H.8-azurin, and Laz in toxicity studies and glioblastoma therapy in preclinical and human clinical trials.
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Kretchmer, Joshua S., Nicholas Boekelheide, Jeffrey J. Warren, Jay R. Winkler, Harry B. Gray, and Thomas F. Miller. "Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein." Proceedings of the National Academy of Sciences 115, no. 24 (May 29, 2018): 6129–34. http://dx.doi.org/10.1073/pnas.1805719115.

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We combine experimental and computational methods to address the anomalous kinetics of long-range electron transfer (ET) in mutants of Pseudomonas aeruginosa azurin. ET rates and driving forces for wild type (WT) and three N47X mutants (X = L, S, and D) of Ru(2,2′-bipyridine)2 (imidazole)(His83) azurin are reported. An enhanced ET rate for the N47L mutant suggests either an increase of the donor–acceptor (DA) electronic coupling or a decrease in the reorganization energy for the reaction. The underlying atomistic features are investigated using a recently developed nonadiabatic molecular dynamics method to simulate ET in each of the azurin mutants, revealing unexpected aspects of DA electronic coupling. In particular, WT azurin and all studied mutants exhibit more DA compression during ET (>2 Å) than previously recognized. Moreover, it is found that DA compression involves an extended network of hydrogen bonds, the fluctuations of which gate the ET reaction, such that DA compression is facilitated by transiently rupturing hydrogen bonds. It is found that the N47L mutant intrinsically disrupts this hydrogen-bond network, enabling particularly facile DA compression. This work, which reveals the surprisingly fluctional nature of ET in azurin, suggests that hydrogen-bond networks can modulate the efficiency of long-range biological ET.
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Ortega, Vilhena, Zotti, Díez-Pérez, Cuevas, and Pérez. "Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations." Biomolecules 9, no. 10 (October 15, 2019): 611. http://dx.doi.org/10.3390/biom9100611.

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In the growing field of biomolecular electronics, blue-copper Azurin stands out as one of the most widely studied protein in single-molecule contacts. Interestingly, despite the paramount importance of the structure/dynamics of molecular contacts in their transport properties, these factors remain largely unexplored from the theoretical point of view in the context of single Azurin junctions. Here we address this issue using all-atom Molecular Dynamics (MD) of Pseudomonas Aeruginosa Azurin adsorbed to a Au(111) substrate. In particular, we focus on the structure and dynamics of the free/adsorbed protein and how these properties are altered upon single-point mutations. The results revealed that wild-type Azurin adsorbs on Au(111) along two well defined configurations: one tethered via cysteine groups and the other via the hydrophobic pocket surrounding the Cu 2 + . Surprisingly, our simulations revealed that single amino-acid mutations gave rise to a quenching of protein vibrations ultimately resulting in its overall stiffening. Given the role of amino-acid vibrations and reorientation in the dehydration process at the protein-water-substrate interface, we suggest that this might have an effect on the adsorption process of the mutant, giving rise to new adsorption configurations.
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Dissertations / Theses on the topic "Azurin protein"

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Manesis, Anastasia C. "Bioorganometallic Chemistry within Nickel-Substituted Azurin: From Protein Design to Reactivity." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1542735809462775.

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Peters-Libeu, Clare Ann. "Structural and electrostatic contributions to differences in oxidation-reduction potentials of two mutants of the copper protein, pseudoazurin /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/5683.

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Nour, El Din Suzanne [Verfasser]. "Azurin (P28) fusion protein mediated photodynamic therapy in the treatment of malignant tumors / Suzanne Nour El Din." Ulm : Universität Ulm, 2017. http://d-nb.info/1140118137/34.

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Mizzon, Giulia. "Bioelectrochemistry by fluorescent cyclic voltammetry." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:6a1134dd-c24d-4e60-ac83-936a6918131f.

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Understanding the factors influencing the ET characteristics of redox proteins confined at an electrochemical interface is of fundamental importance from both pure (fundamental science) and applied (biosensory) perspectives. This thesis reports on progress made in the emerging field of coupled electrochemical characterization and optical imaging in moving the analysis of redox-active films to molecular scales. More specifically the combination of cyclic voltammetry and wide-field Total Internal Reflection (TIRF) microscopy, here named ‘Fluorescent Cyclic Voltammetry’ (FCV), was applied to monitoring the response of surface-confined redox active proteins at submonolayer concentrations. The combined submicrometre spatial resolution and photon capture efficiency of an inverted TIRF configuration enabled the redox reactions of localized populations of proteins to be directly imaged at scales down to a few hundreds of molecules. This represents a 6-9 orders of magnitude enhancement in sensitivity with respect to classical current signals observed in bioelectrochemical analysis. Importantly, measurements of redox potentials at this scale could be achieved from both natural and artificially designed bioelectrochemical fluorescent switches and shed fundamental light on the thermodynamic and kinetic dispersion within a population of surface confined metalloproteins. The first three chapters of this thesis provide an overview of the relevant literature and a theoretical background to both the rapidly expanding fields of electroactive monolayers bioelectrochemistry and TIRF imaging. The initial design and construction of a robust electrochemically and optically addressable fluorescent switch, crucial to the applicability of FCV is reported in chapter 5. The generation of optically transparent, and chemically modifiable electrode surfaces suitable for FCV are also described. Chapter 6 describes the response of the surface confined azurin-based switch. Analysis of the spatially-resolved redox reaction of zeptomole samples in various conditions enables the mapping of thermodynamic dispersion across the sampled areas. In chapter 7 the newly developed FCV detection method was extended to investigate more complex bioelectrochemical systems containing multiple electron transferring redox centres and responding optically at different wavelengths. This approach provides a platform for spectral resolution of different electrochemical processes on the same sample. Finally in chapter 8 an electrochemical procedure is proposed for investigating the kinetic response of redox proteins using a fundamentally new methodology based on interfacial capacitance. In using variations in the surface chemistry to tune the rate of electron transfer, the approach was shown to be a robust and facile means of characterising redox active films in considerably more detail than possible through standard electrochemical methodologies. Ultimately, it can be applied to probe dispersion within protein populations and represents a powerful means of analysing molecular films more generally.
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Harris, Roger Lyndon. "Studies in intermolecular electron transfer between the copper-containing proteins azurin I and nitrate reductase from Alcaligenes xylosoxidans." Thesis, University of East Anglia, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399795.

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Kalyani, Neeti. "Azurin protein for the development of bionanodevices." Thesis, 2018. http://localhost:8080/xmlui/handle/12345678/7696.

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"Folding of azurin: A copper-binding beta-barrel protein." Tulane University, 2002.

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In this body of work, studies of folding kinetics and thermodynamic stability of Pseudomonas aeruginosa azurin, a copper-binding beta-barrel protein, are presented. To uncover the role of the copper cofactor in determining the folding pathway of azurin, interactions of the unfolded protein with copper were investigated using a mutagenic approach and a model-peptide system. Based on the findings, the coordination sphere of copper in the unfolded protein is proposed to involve at least two native-state ligands: histidine-117 and cysteine-112. A small peptide corresponding to the carboxy-terminal part of full-length azurin is found to adopt beta-sheet-like structure upon copper binding, Formation of this beta-hairpin induced by the copper ion in the unfolded protein was originally suggested as a mechanism for folding nucleation. However, detailed folding-kinetic studies demonstrate that the folding speed of azurin is not increased in the presence of copper. It is concluded that formation of the beta-hairpin induced by copper binding is not rate limiting for folding The topology of the native state is the primary determinant of the folding rate for azurin, as demonstrated by the study of two active-site azurin mutants. His46Gly and His117Gly azurins, in their apo (without cofactor) forms. The decreases in the thermodynamic stability of the mutants, as compared to wild-type azurin, originate from the acceleration of unfolding, However, the folding rates for the mutants are almost identical to what is observed for wild-type apo-azurin
acase@tulane.edu
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張慈芳. "Physiological function and transcription regulation of Azurin, a redox protein in Pseudomonas aeruginosa PAO1." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/72838359500788603865.

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Abreu, Sofia de Almeida Santos de Castro e. "Bacterial protein azurin as a new candidate anticancer drug by decreasing cell adhesion through integrins." Master's thesis, 2013. http://hdl.handle.net/10316/24731.

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Dissertação de mestrado em Biologia Celular e Molecular,apresentada ao Departamento de Ciências da Vida da Faculdade de Ciências e Tecnologia da Universidade de Coimbra.
A azurina é uma proteína de 14 kDa produzida por Pseudomonas aeruginosa, com actividade citotóxica em linhas celulares cancerígenas humanas. A azurina entra preferencialmente em células cancerígenas, formando um complexo com a proteína supressora tumoral p53, estabilizando-a e induzindo a apoptose. A capacidade de migração e invasão deve-se, em parte, à regulação de proteínas de adesão celular, como a P-caderina. A Pcaderina é sobre-expressa em 30% dos cancros de mama e é um marcador de mau prognóstico. Por isso, a P-caderina é um potencial alvo terapêutico em cancro de mama. Por essa razão, a capacidade da azurina diminuir esta proteína em modelos de cancro de mama que sobre-expressam P-caderina foi testada, verificando-se que a azurina diminui a sua expressão proteica e localização membranar. No entanto, o mecanismo de acção da azurina não é ainda bem conhecido. Por outro lado, o cancro do pulmão tem vias de sinalização semelhantes associadas à adesão celular, e por isso, este trabalho também se foca no impacto da azurina no cancro de pulmão. Não se sabe muito sobre como o microambiente estromal em locais de metástase fornece um ambiente adequado para as células tumorais. É por isso importante estudar a interação entre células metastáticas e o meio extracelular. Diferentes linhas celulares de cancro de mama com níveis distintos de expressão de Pcaderina e diferentes capacidades invasivas (MCF-7/AZ.Mock, MCF-7/AZ.Pcad, SUM149, BT- 20) e de cancro do pulmão (A549) foram tratadas com azurina (50μM e 100μM). O efeito de azurina na adesão celular com diferentes componentes do meio extracelular (laminina-332, colagénio do tipo-I, fibronectina e colagénio do tipo-IV) foi investigado, bem como a expressão de subunidades de integrina (α6, β1 e β4) por western blot. Os efeitos da azurina também foram avaliados por outros parâmetros, tais como a medição de ROS, imunocitoquímica, zimografia de gelatina de modo a avaliar a actividade da MMP-2 e a capacidade de invasão. A azurina diminui a expressão das subunidades de integrina (α6, β1 e β4) em todos os modelos estudados (cancro de mama e de pulmão), de forma mais consistente na subunidade de integrina β1. Além disso, a azurina diminui a adesão celular a componentes da matriz extracelular, principalmente em colagénio e laminina (cancro da mama) e fibronectina (cancro de pulmão), os componentes principais de cada tipo de cancro. Em BT-20 e A549, a azurina diminui a actividade da MMP-2 e, consequentemente, a capacidade de invasão. Estes resultados confirmam a azurina como um potencial fármaco terapêutico no cancro.
Azurin is a 14 kDa protein produced by Pseudomonas aeruginosa which has cytotoxicity activity towards human cancer cell lines. Azurin can enter preferentially into cancer cells, forming a complex with the tumour suppressor p53, stabilizing it and inducing apoptosis. The capacity of migration and invasion is due, in part, to the regulation of adhesion proteins, like Pcadherin. P-cadherin is over-expressed in 30% of breast cancers and it is a marker of poor survival. Therefore, P-cadherin is a potential therapeutic target in breast cancer. For that reason, azurin was used to target P-cadherin, decreasing its level in P-cadherin over-expressing breast cancer models and membranar localisation. However, the mechanism of action of azurin is not well known. On the other hand, lung cancer has similar signalling pathways associated with adhesion, and therefore, this work also focuses on the impact of azurin in lung cancer. Not much is known about how the stromal microenvironment at metastasis sites provides a suitable home to tumour cells. It is important to study the interaction between metastatic cells and ECM. We treated different cancer cells models with azurin (50 μM and 100 μM): four breast cancer cell lines with distinct levels of P-cadherin expression and different invasive capacities (MCF- 7/AZ.Mock, MCF-7/AZ.Pcad, SUM149 and BT-20) and one non-small cell lung cancer cell line (A549). We investigated the effect of azurin in cell adhesion with different ECM components (laminin-332, collagen type-I, fibronectin and collagen type-IV) and we also investigated integrin subunits (α6, β1 and β4) expression by western blot. The azurin effects were also evaluated by others parameters, such as ROS measurement, immunocytochemistry, gelatine zymography to evaluate MMP-2 activity and invasion capacity. Azurin decreased integrin subunits (α6, β1 and β4) in all studied models (breast and lung cancer), more consistently in the integrin subunit β1. Moreover, azurin decreased adhesion to ECM components, with more significance in collagen and laminin (breast cancer) and fibronectin (lung cancer), both main components in each cancer type. In BT-20 and A549, azurin decreased MMP-2 activity and the invasion through MatrigelTM. All these results corroborate azurin as potential cancer therapeutic drug.
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Silva, Gonçalo Emanuel Fialho Mourata da 1989. "Discovering and exploiting bacterial proteins as anticancer agents." Master's thesis, 2013. http://hdl.handle.net/10451/9665.

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Tese de mestrado. Biologia (Biologia Humana e Ambiente). Universidade de Lisboa, Faculdade de Ciências, 2013
Azurin is a low molecular weight protein, produced by Pseudomonas aeruginosa and possesses several antitumor properties, like causing P-cadherin levels to decrease in invasive breast cancer cells. In this work, we studied the effect of lysosome and proteasome inhibitors on P-cadherin level, using a breast cancer cell line, expressing high P-cadherin level (MCF-7/AZ.Pcad), previously treated with azurin. Additionally, we evaluated how a cholesterol-depleting agent (MβCD) affects P-cadherin level. The effects of both inhibitors on P-cadherin were observed by western blot and confirmed that azurin mediates P-cadherin degradation through lysosome and proteasome proteolytic pathways. We also described, for the first time, that MβCD causes P-cadherin level to decrease. Together, these findings have increased our understanding of how the bacterial protein azurin is acting as anti-cancer agent. In this work we have also studied the in vitro cytotoxicity of two other bacterial proteins (MPT 63 and Ndk) against human breast and lung cancer cells. MPT 63 is an antigen secreted by Mycobacterium tuberculosis that induces immunogenic responses in animal models and its cytotoxicity against several tumor cell lines was recently described in a patent. Nucleoside diphosphate kinase (Ndk) is a ubiquitous enzyme which maintains the nucleotide pools within the cells, and can be secreted by P. aeruginosa. A human Ndk, termed Nm23-H1, also showed an anti-metastatic role in different cancer models. In order to test possible antitumor properties of these proteins, MTT cell viability assays were performed in breast and lung cancer models (MCF-7/AZ.Mock and A549) using increasing azurin, MPT 63 and Ndk concentrations, and different exposure times. In addition, matrigel invasion assay was performed in A549 invasive cells treated with Ndk. Both azurin, MPT 63 and Ndk evidenced cytotoxicity against both cancer models in a time and dose dependent manner. Ndk revealed cytotoxic activity and selectivity against tumor cells similar to azurin. We observed a small decrease in cell invasion using this protein. In summary, we promoted a screening of new bacterial proteins that demonstrated antitumor potential, especially Ndk.
Novas terapias anti-tumorais emergentes baseiam-se em abordagens pouco convencionais, como a utilização de microorganismos, nomeadamente bactérias vivas ou produtos purificados a partir das mesmas, como proteínas. A azurina é uma proteína de baixo peso molecular, produzida por Pseudomonas aeruginosa e possui diversas propriedades anti-tumorais, entre as quais a indução de apoptose em células tumorais pela estabilização da proteína supressora de tumores p53. Mais recentemente, um novo tipo de acção anti-tumoral foi descoberta, tendo sida descrita a sua capacidade de diminuir os níveis de P-caderina em células tumorais invasivas de cancro da mama, sem afectar, no entanto, os níveis de E-caderina. O mecanismo, pelo qual a azurina causa o decréscimo de P-caderina nas células tumorais não é ainda totalmente conhecido, mas esta parece actuar a nível pós-transcripcional dado que não se verificam diferenças na expressão de P-caderina em células tratadas com azurina. Dados relativos a ensaios com análise a microarrays revelaram que a transcrição de genes associados ao lisossoma e processos de transporte mediado por vesículas se encontrava mais activa. No presente trabalho pretendeu-se esclarecer se a diminuição dos níveis de P-caderina, mediada pela acção da azurina, se deve à sua degradação pelos sistemas proteolíticos a nível celular, como o lisossoma e proteossoma. Nesse sentido utilizaram-se células de uma linha celular de cancro da mama, que expressa níveis elevados de P-caderina (MCF-7/AZ.Pcad), e que foram previamente tratadas com azurina antes de serem administrados inibidores de lisossoma (cloreto de amónio) e de proteossoma (MG-132). Do mesmo modo foram também avaliados os efeitos de um agente sequestrador de colesterol (MβCD) e inibidor de entrada da azurina nas células, ao nível da P-caderina nesta linha celular tumoral. Os efeitos de ambos os inibidores, ao nível da degradação da P-caderina, foram observados por western blot e confirmaram que a azurina medeia a degradação da P-caderina por sistemas proteolíticos como o lisossoma e o proteossoma. Descrevemos igualmente, pela primeira vez, que a MβCD provoca a diminuição dos níveis de P-caderina sem afectar os níveis de E-caderina. Conjuntamente, estes resultados permitiram aumentar o nosso conhecimento acerca do modo como a azurina actua como agente anticancerígeno neste caso específico. Neste trabalho pretendemos também estudar a citotoxicidade in vitro de duas outras proteínas bacterianas (MPT 63 e Ndk) em células tumorais humanas de cancro da mama e de pulmão. A MPT 63 é uma proteína antigénica secretada por Mycobacterium tuberculosis e capaz de induzir respostas imunogénicas em diversos modelos animais. Esta proteína apresenta uma estrutura semelhante a imunoglobulinas, uma característica que é partilhada com a azurina. Recentemente foi descrita como possuindo elevada actividade citotóxica contra várias linhas celulares tumorais, assim como um péptido derivado desta proteína (MB30), tendo esta propriedade de ambas as molécula sido registada numa patente. A nucleosídeo difosfato cinase (Ndk) é uma enzima ubíqua em diversos organismos e que tem como função manter as reservas de nucleótidos das células. Esta proteína pode igualmente ser secretada por várias bactérias como P. aeruginosa. As Ndks humanas estão agrupadas numa família de proteínas denominada de Nm23, tendo sidas até hoje descritas dez tipos. A primeira destas proteínas a ser descrita, denominada Nm23-H1, demonstrou possuir adicionalmente uma importante acção anti-metastática em diferentes modelos de cancro. Tendo em conta o vasto leque de acção anti-tumoral da azurina, procurou-se seleccionar duas proteínas bacterianas (MPT 63 e Ndk) com propriedades interessantes de serem exploradas, no sentido de testar uma possível actividade citotóxica das mesmas em células cancerígenas. Para esse efeito foram realizados ensaios de viabilidade celular (ou ensaios de MTT) em modelos tumorais de cancro da mama e do pulmão (MCF-7/AZ.Mock e A549), usando concentrações crescentes de azurina, MPT 63 e Ndk, bem como diferentes tempos de exposição, com o intuito de entender como estes parâmetros podem afectar o nível de citotoxicidade destas proteínas. Adicionalmente foi testada a actividade anti-metastática da Ndk, realizando um ensaio de invasão em matrigel, usando uma linha celular altamente invasiva de cancro de pulmão, A549. A azurina, assim como a MPT 63 e a Ndk, evidenciaram citotoxicidade contra ambos os modelos tumorais testados, de um modo dependente do tempo e concentrações administradas. A Ndk revelou níveis de actividade citotóxica e selectividade de acção, relativamente a células tumorais, semelhantes à azurina. Observámos ainda um pequeno decréscimo da invasão celular das células tumorais de pulmão A549, quando esta proteína foi administrada. Em suma, promovemos um rastreio de novas proteínas bacterianas que demonstraram potencial anti-tumoral, especialmente a Ndk. O conhecimento acerca destas propriedades necessita de ser expandido e aprofundado para que, no futuro, se possa avaliar a sua utilização como agentes anti-cancerígenos úteis, tal como a azurina.
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Books on the topic "Azurin protein"

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Freato, Roberto. Microsoft Azure Security: Protect Your Solutions from Malicious Users Using Microsoft Azure Services. Packt Publishing, Limited, 2015.

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Book chapters on the topic "Azurin protein"

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Strambini, Giovanni B. "Fluorescence and Phosphorescence Methods to Probe Protein Structure and Stability in Ice: The Case of Azurin." In Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals, 207–29. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470595886.ch9.

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Mrozek, Dariusz. "Azure Cloud Services." In Scalable Big Data Analytics for Protein Bioinformatics, 51–67. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-98839-9_3.

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Mrozek, Dariusz. "Scaling 3D Protein Structure Similarity Searching with Azure Cloud Services." In Scalable Big Data Analytics for Protein Bioinformatics, 69–102. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-98839-9_4.

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Mrozek, Dariusz. "Scalable Prediction of Intrinsically Disordered Protein Regions with Spark Clusters on Microsoft Azure Cloud." In Scalable Big Data Analytics for Protein Bioinformatics, 215–47. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-98839-9_9.

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Ambi Karthikeyan, Shijimol. "Security: Protect Your Workloads in the Cloud." In Demystifying the Azure Well-Architected Framework, 105–30. Berkeley, CA: Apress, 2021. http://dx.doi.org/10.1007/978-1-4842-7119-3_6.

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Małysiak-Mrozek, Bożena, Paweł Daniłowicz, and Dariusz Mrozek. "Efficient 3D Protein Structure Alignment on Large Hadoop Clusters in Microsoft Azure Cloud." In Beyond Databases, Architectures and Structures. Facing the Challenges of Data Proliferation and Growing Variety, 33–46. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-99987-6_3.

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Mrozek, Dariusz, Tomasz Kutyła, and Bożena Małysiak-Mrozek. "Accelerating 3D Protein Structure Similarity Searching on Microsoft Azure Cloud with Local Replicas of Macromolecular Data." In Parallel Processing and Applied Mathematics, 254–65. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-32152-3_24.

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Garizo, Ana Rita, Nuno Bernardes, Ananda M. Chakrabarty, and Arsénio M. Fialho. "The Anticancer Potential of the Bacterial Protein Azurin and Its Derived Peptide p28." In Microbial Infections and Cancer Therapy, 319–38. Jenny Stanford Publishing, 2019. http://dx.doi.org/10.1201/9781351041904-9.

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Mrozek, Dariusz. "Cloud-Based Computing Architectures for Solving Hot Issues in Structural Bioinformatics." In Biotechnology, 322–43. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-8903-7.ch012.

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Abstract:
Bioinformatics as a scientific domain develops tools that enable understanding the wealth of information hidden in huge volumes of biological data. However, there are several problems in bioinformatics that, although already solved or at least equipped with promising algorithms, still require huge computing power in order to be completed in a reasonable time. Cloud computing responds to these demands. This chapter shows several cloud-based computing architectures for solving hot issues in structural bioinformatics, such as protein structure similarity searching or 3D protein structure prediction. Presented architectures have been implemented in Microsoft Azure public cloud and tested in several projects developed by Cloud4Proteins research group.
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Mrozek, Dariusz. "Cloud-Based Computing Architectures for Solving Hot Issues in Structural Bioinformatics." In Advances in Systems Analysis, Software Engineering, and High Performance Computing, 294–314. IGI Global, 2015. http://dx.doi.org/10.4018/978-1-4666-8213-9.ch009.

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Abstract:
Bioinformatics as a scientific domain develops tools that enable understanding the wealth of information hidden in huge volumes of biological data. However, there are several problems in bioinformatics that, although already solved or at least equipped with promising algorithms, still require huge computing power in order to be completed in a reasonable time. Cloud computing responds to these demands. This chapter shows several cloud-based computing architectures for solving hot issues in structural bioinformatics, such as protein structure similarity searching or 3D protein structure prediction. Presented architectures have been implemented in Microsoft Azure public cloud and tested in several projects developed by Cloud4Proteins research group.
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Conference papers on the topic "Azurin protein"

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Petrich, J. W., J. W. Longworth, and G. R. Fleming. "Electron Transfer in Homologous Azurins." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.tuf7.

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Using time correlated single photon counting, we have studied electron transfer rates, kET in the homologous blue-copper proteins, azurins, obtained from Pseudomonas aeruginosa (Pae) and Alcaligenes faecalis (Afe). The salient difference between these proteins lies in the position of their single tryptophan residues. The tryptophan in azurin Pae, W48, is buried in the hydrophobic core of the protein while the tryptophan in azurin Afe, W118, lies on the protein surface, exposed to the solvent [1]. kET for the reaction W* + Az-Cu (II)→W*+·+Az-Cu(I) was determined to be 1 × 1010 s−1 and 0.5 × 1010s−1 for Pae and Afe, respectively ; i.e. kET(W48)/kET(W118) = 2.
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Rusmerryani, Micke, Masako Takasu, Kazutomo Kawaguchi, Hiroaki Saito, and Hidemi Nagao. "Protein–Protein Interactions of Azurin Complex by Coarse-Grained Simulations with a Gō-Like Model." In Proceedings of the 12th Asia Pacific Physics Conference (APPC12). Journal of the Physical Society of Japan, 2014. http://dx.doi.org/10.7566/jpscp.1.012054.

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Bernardes, Nuno, Ana Sofia Ribeiro, Raquel Seruca, Joana Paredes, and Arsenio M. Fialho. "Bacterial protein azurin as a new candidate drug to treat untreatable breast cancers." In 2011 1st Portuguese Meeting in Bioengineering ¿ The Challenge of the XXI Century (ENBENG). IEEE, 2011. http://dx.doi.org/10.1109/enbeng.2011.6026047.

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