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[PMID]: 28931274 [Au] Autor: Damont A; Boisgard R; Dollé F; Hollocou M; Kuhnast B [Ad] Endereço: IMIV, Service Hospitalier Frédéric Joliot, CEA, Inserm, Université Paris Sud, CNRS, Université Paris-Saclay , Orsay, France. [Ti] Título: Avidin/Biotin Bioinspired Platform for Dual In Vivo F-PET/NIRF Molecular Imaging. [So] Source: Bioconjug Chem;28(10):2524-2529, 2017 Oct 18. [Is] ISSN: 1520-4812 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The complementary nature of positron emission tomography (PET) and near-infrared fluorescence (NIRF) imaging makes the development of innovative multimodal PET/NIRF probes a very exciting prospect. Herein, the bioinspired design of novel platform exploiting the strength and specificity of interactions between radioactive and fluorescent biotin derivatives and an avidin core is reported. The combination of an original [ F]fluoropyridinylated-biotin derivative and commercially available fluorescent biotin derivatives (Atto-425 and Atto-680) is investigated. The in vivo distribution of such a customized platform is also reported, for the first time, in healthy rodent using PET and ex vivo fluorescence imaging. [Mh] Termos MeSH primário: Avidina/metabolismo Biomimética/métodos Biotina/metabolismo Radioisótopos de Flúor Raios Infravermelhos Imagem Óptica/métodos Tomografia por Emissão de Pósitrons/métodos [Mh] Termos MeSH secundário: Radioquímica [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Fluorine Radioisotopes); 1405-69-2 (Avidin); 6SO6U10H04 (Biotin) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171107 [Lr] Data última revisão: 171107 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170922 [St] Status: MEDLINE [do] DOI: 10.1021/acs.bioconjchem.7b00536

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[PMID]: 28846388 [Au] Autor: Hammink R; Eggermont LJ; Zisis T; Tel J; Figdor CG; Rowan AE; Blank KG [Ad] Endereço: Department of Molecular Materials, Institute for Molecules and Materials, Radboud University , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. [Ti] Título: Affinity-Based Purification of Polyisocyanopeptide Bioconjugates. [So] Source: Bioconjug Chem;28(10):2560-2568, 2017 Oct 18. [Is] ISSN: 1520-4812 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Water-soluble polyisocyanopeptides (PICs) are a new class of synthetic polymers that mimic natural protein-based filaments. Their unique semiflexible properties combined with a length of several hundred nanometers have recently enabled a number of biomedical applications ranging from tissue engineering to cancer immunotherapy. One crucial step toward the further development of PICs for these applications is the efficient and controlled synthesis and purification of PIC-biomolecule conjugates. Considering the large size of PICs and the biomolecules to be conjugated, conjugation reactions do usually not proceed to completion due to steric effects. As a consequence, purification of the reaction mixture is necessary to separate the obtained bioconjugates from unreacted biomolecules. As a direct result of the semiflexible nature of PICs, standard polymer and protein purification methods based on molecular weight have not been successful. Here, we introduce a new affinity-based purification method utilizing biotin as an affinity tag. PICs decorated with a controlled and tunable density of biotin molecules (biotinPICs) were efficiently bound to and eluted from a monoavidin resin in buffered aqueous solution. Using these biotinPICs, two different protein conjugates were synthesized, one carrying the enzyme alkaline phosphatase (PhoA) and the other T-cell activating anti-CD3 antibodies. The resulting biotinPIC-protein conjugates were successfully obtained in high purity (>90%) and without any loss of protein activity. The high purity greatly simplifies the analysis of biotinPIC bioconjugates, such as the determination of the average number of biomolecules conjugated per biotinPIC chain. Most importantly, it allows for the direct and straightforward application of the obtained bioconjugates in the desired applications. The new method developed may further be adapted for the purification of other advanced bioconjugates that are difficult to obtain in high purity with the available standard methods. [Mh] Termos MeSH primário: Dipeptídeos/química Dipeptídeos/isolamento & purificação Nitrilos/química Nitrilos/isolamento & purificação [Mh] Termos MeSH secundário: Fosfatase Alcalina/metabolismo Animais Anticorpos Monoclonais/química Anticorpos Monoclonais/imunologia Avidina/química Avidina/metabolismo Biotina/química Complexo CD3/imunologia Escherichia coli/enzimologia Seres Humanos Imunoconjugados/química Imunoconjugados/isolamento & purificação Solubilidade Água/química [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antibodies, Monoclonal); 0 (CD3 Complex); 0 (Dipeptides); 0 (Immunoconjugates); 0 (Nitriles); 0 (poly(isocyanodipeptide)); 059QF0KO0R (Water); 1405-69-2 (Avidin); 6SO6U10H04 (Biotin); EC 3.1.3.1 (Alkaline Phosphatase) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170829 [St] Status: MEDLINE [do] DOI: 10.1021/acs.bioconjchem.7b00398

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[PMID]: 28765707 [Au] Autor: Liu Y; Wu X; Sun X; Wang D; Zhong Y; Jiang D; Wang T; Yu D; Zhang N [Ad] Endereço: School of Pharmaceutical Science, Shandong University. [Ti] Título: Design, synthesis, and evaluation of VEGFR-targeted macromolecular MRI contrast agent based on biotin-avidin-specific binding. [So] Source: Int J Nanomedicine;12:5039-5052, 2017. [Is] ISSN: 1178-2013 [Cp] País de publicação: New Zealand [La] Idioma: eng [Ab] Resumo: Developing magnetic resonance imaging (MRI) contrast agents with high relaxivity and specificity was essential to increase MRI diagnostic sensitivity and accuracy. In this study, the MRI contrast agent, vascular endothelial growth factor receptor (VEGFR)-targeted poly (l-lysine) (PLL)-diethylene triamine pentacetate acid (DTPA)-gadolinium (Gd) (VEGFR-targeted PLL-DTPA-Gd, VPDG), was designed and prepared to enhance the MRI diagnosis capacity of tumor. Biotin-PLL-DTPA-Gd was synthesized first, then, VEGFR antibody was linked to biotin-PLL-DTPA-Gd using biotin-avidin reaction. In vitro cytotoxicity study results showed that VPDG had low toxicity to MCF-7 cells and HepG2 cells at experimental concentrations. In cell uptake experiments, VPDG could significantly increase the internalization rates (61.75%±5.22%) in VEGFR-positive HepG2 cells compared to PLL-DTPA-Gd (PDG) (25.16%±4.71%, <0.05). In MRI studies in vitro, significantly higher T1 relaxivity (14.184 mM s ) was observed compared to Magnevist (4.9 mM s ; <0.01). Furthermore, in vivo MRI study results showed that VPDG could significantly enhance the tumor signal intensity and prolong the diagnostic time (from <1 h to 2.5 h). These results indicated that macromolecular VPDG was a promising MRI contrast agent and held great potential for molecular diagnosis of tumor. [Mh] Termos MeSH primário: Meios de Contraste/química Imagem por Ressonância Magnética/métodos Neoplasias Experimentais/diagnóstico por imagem Receptores de Fatores de Crescimento do Endotélio Vascular/metabolismo [Mh] Termos MeSH secundário: Animais Avidina/química Avidina/metabolismo Biotina/química Biotina/metabolismo Meios de Contraste/síntese química Gadolínio/química Gadolínio DTPA Células Hep G2 Seres Humanos Células MCF-7 Camundongos Ácido Pentético/química Poliaminas/química Polilisina/química [Pt] Tipo de publicação: EVALUATION STUDIES; JOURNAL ARTICLE [Nm] Nome de substância: 0 (Contrast Media); 0 (Polyamines); 03K6SX4V2J (diethylenetriamine); 1405-69-2 (Avidin); 25104-18-1 (Polylysine); 6SO6U10H04 (Biotin); 7A314HQM0I (Pentetic Acid); AU0V1LM3JT (Gadolinium); EC 2.7.10.1 (Receptors, Vascular Endothelial Growth Factor); K2I13DR72L (Gadolinium DTPA) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171030 [Lr] Data última revisão: 171030 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170803 [St] Status: MEDLINE [do] DOI: 10.2147/IJN.S131878

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[PMID]: 28636798 [Au] Autor: Piontek A; Witte C; May Rose H; Eichner M; Protze J; Krause G; Piontek J; Schröder L [Ad] Endereço: Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Structural Bioinformatics and Protein Design, Berlin, Germany. [Ti] Título: A cCPE-based xenon biosensor for magnetic resonance imaging of claudin-expressing cells. [So] Source: Ann N Y Acad Sci;1397(1):195-208, 2017 Jun. [Is] ISSN: 1749-6632 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The majority of malignant tumors originate from epithelial cells, and many of them are characterized by an overexpression of claudins (Cldns) and their mislocalization out of tight junctions. We utilized the C-terminal claudin-binding domain of Clostridium perfringens enterotoxin (cCPE), with its high affinity to specific members of the claudin family, as the targeting unit for a claudin-sensitive cancer biosensor. To overcome the poor sensitivity of conventional relaxivity-based magnetic resonance imaging (MRI) contrast agents, we utilized the superior sensitivity of xenon Hyper-CEST biosensors. We labeled cCPE for both xenon MRI and fluorescence detection. As one readout module, we employed a cryptophane (CrA) monoacid and, as the second, a fluorescein molecule. Both were conjugated separately to a biotin molecule via a polyethyleneglycol chemical spacer and later via avidin linked to GST-cCPE. Nontransfected HEK293 cells and HEK293 cells stably expressing Cldn4-FLAG were incubated with the cCPE-based biosensor. Fluorescence-based flow cytometry and xenon MRI demonstrated binding of the biosensor specifically to Cldn4-expressing cells. This study provides proof of concept for the use of cCPE as a carrier for diagnostic contrast agents, a novel approach for potential detection of Cldn3/-4-overexpressing tumors for noninvasive early cancer detection. [Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos Claudina-4/metabolismo Enterotoxinas/metabolismo Imagem por Ressonância Magnética/métodos Xenônio/química [Mh] Termos MeSH secundário: Avidina/química Claudina-3/química Claudina-3/genética Claudina-3/metabolismo Claudina-4/química Claudina-4/genética Enterotoxinas/química Enterotoxinas/genética Citometria de Fluxo Fluoresceínas/química Células HEK293 Seres Humanos Microscopia Confocal Modelos Moleculares Compostos Policíclicos/química Polietilenoglicóis/química Ligação Proteica Estrutura Terciária de Proteína Reprodutibilidade dos Testes [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Claudin-3); 0 (Claudin-4); 0 (Enterotoxins); 0 (Fluoresceins); 0 (Polycyclic Compounds); 0 (cryptophane A); 0 (enterotoxin, Clostridium); 1405-69-2 (Avidin); 30IQX730WE (Polyethylene Glycols); 3H3U766W84 (Xenon) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170822 [Lr] Data última revisão: 170822 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170622 [St] Status: MEDLINE [do] DOI: 10.1111/nyas.13363

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[PMID]: 28590137 [Au] Autor: Hedglin M; Aitha M; Benkovic SJ [Ad] Endereço: Department of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States. [Ti] Título: Monitoring the Retention of Human Proliferating Cell Nuclear Antigen at Primer/Template Junctions by Proteins That Bind Single-Stranded DNA. [So] Source: Biochemistry;56(27):3415-3421, 2017 Jul 11. [Is] ISSN: 1520-4995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: In humans, proliferating cell nuclear antigen (PCNA) sliding clamps encircling DNA coordinate various aspects of DNA metabolism throughout the cell cycle. A critical aspect of this is restricting PCNA to the vicinity of its DNA target site. For example, PCNA must be maintained at or near primer/template (P/T) junctions during DNA synthesis. With a diverse array of cellular factors implicated, many of which interact with PCNA, DNA, or both, it is unknown how this critical feat is achieved. Furthermore, current biochemical assays that examine the retention of PCNA near P/T junctions are inefficient, discontinuous, and qualitative and significantly deviate from physiologically relevant conditions. To overcome these challenges and limitations, we recently developed a novel and convenient Förster resonance energy transfer (FRET) assay that directly and continuously monitors the retention of human PCNA at a P/T junction. Here we describe in detail the design, methodology, interpretation, and limitations of this quantitative FRET assay using the single-stranded DNA-binding protein, SSB, from Escherichia coli as an example. This powerful tool is broadly applicable to any single-stranded DNA-binding protein and may be utilized and/or expanded upon to dissect DNA metabolic pathways that are dependent upon PCNA. [Mh] Termos MeSH primário: Primers do DNA/metabolismo DNA de Cadeia Simples/metabolismo Proteínas de Ligação a DNA/metabolismo Proteínas de Escherichia coli/metabolismo Modelos Moleculares Antígeno Nuclear de Célula em Proliferação/metabolismo Proteína de Replicação A/metabolismo [Mh] Termos MeSH secundário: Avidina/química Avidina/metabolismo Sítios de Ligação Biotina/química Biotina/metabolismo Carbocianinas/química Primers do DNA/química Replicação do DNA DNA de Cadeia Simples/química Proteínas de Ligação a DNA/química Proteínas de Ligação a DNA/genética Proteínas de Escherichia coli/química Proteínas de Escherichia coli/genética Transferência Ressonante de Energia de Fluorescência Corantes Fluorescentes/química Seres Humanos Microscopia de Fluorescência Conformação Molecular Mutação Fragmentos de Peptídeos/química Fragmentos de Peptídeos/genética Fragmentos de Peptídeos/metabolismo Antígeno Nuclear de Célula em Proliferação/química Antígeno Nuclear de Célula em Proliferação/genética Domínios e Motivos de Interação entre Proteínas Estabilidade Proteica Proteínas Recombinantes/química Proteínas Recombinantes/metabolismo Proteína de Replicação A/química Proteína de Replicação A/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Carbocyanines); 0 (Cys5 label); 0 (DNA Primers); 0 (DNA, Single-Stranded); 0 (DNA-Binding Proteins); 0 (Escherichia coli Proteins); 0 (Fluorescent Dyes); 0 (Peptide Fragments); 0 (Proliferating Cell Nuclear Antigen); 0 (RPA1 protein, human); 0 (Recombinant Proteins); 0 (Replication Protein A); 0 (SSB protein, E coli); 0 (neutravidin); 1405-69-2 (Avidin); 6SO6U10H04 (Biotin) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 171101 [Lr] Data última revisão: 171101 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170608 [St] Status: MEDLINE [do] DOI: 10.1021/acs.biochem.7b00386

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[PMID]: 28581639 [Au] Autor: Cowell J; Buck M; Essa AH; Clarke R; Vollmer W; Vollmer D; Hilkens CM; Isaacs JD; Hall MJ; Gray J [Ad] Endereço: School of Chemistry, Newcastle University, Newcastle upon Tyne, NE2 7RU, UK. [Ti] Título: Traceless Cleavage of Protein-Biotin Conjugates under Biologically Compatible Conditions. [So] Source: Chembiochem;18(17):1688-1691, 2017 Sep 05. [Is] ISSN: 1439-7633 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Biotinylation of amines is widely used to conjugate biomolecules, but either the resulting label is non-removable or its removal leaves a tag on the molecule of interest, thus affecting downstream processes. We present here a set of reagents (RevAmines) that allow traceless, reversible biotinylation under biologically compatible, mild conditions. Release following avidin-based capture is achieved through the cleavage of a (2-(alkylsulfonyl)ethyl) carbamate linker under mild conditions (200 mm ammonium bicarbonate, pH 8, 16-24 h, room temperature) that regenerates the unmodified amine. The capture and release of biotinylated proteins and peptides from neutravidin, fluorescent labelling through reversible biotinylation at the cell surface and the selective enrichment of proteins from bacterial periplasm are demonstrated. The tags are easily prepared, stable and offer the potential for future application in proteomics, activity-based protein profiling, affinity chromatography and bio-molecule tagging and purification. [Mh] Termos MeSH primário: Biotina/química Proteínas/química [Mh] Termos MeSH secundário: Animais Avidina/química Avidina/metabolismo Biotina/metabolismo Biotinilação Bovinos Cromatografia de Afinidade Corantes Fluorescentes/química Microscopia Confocal Proteínas/metabolismo Proteômica Soroalbumina Bovina/química Soroalbumina Bovina/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Fluorescent Dyes); 0 (Proteins); 0 (neutravidin); 1405-69-2 (Avidin); 27432CM55Q (Serum Albumin, Bovine); 6SO6U10H04 (Biotin) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170606 [St] Status: MEDLINE [do] DOI: 10.1002/cbic.201700214

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[PMID]: 28554074 [Au] Autor: Yenjai S; Kuno M; Samosorn S; Liwporncharoenvong T; Buranaprapuk A [Ad] Endereço: Department of Chemistry, Faculty of Science, Srinakharinwirot University, Sukhumvit 23, Bangkok 10110, Thailand. [Ti] Título: Photochemistry and mechanism of designed pyrenyl probe towards promoted cleavage of proteins. [So] Source: J Photochem Photobiol B;173:35-42, 2017 Aug. [Is] ISSN: 1873-2682 [Cp] País de publicação: Switzerland [La] Idioma: eng [Ab] Resumo: A new photochemical reagent, succinic acid-1(1-pyrene)methylamide (PMA-SUC), was developed to recognize the specific binding sites on model proteins, egg-white lysozyme and avidin. The interaction of the photochemical reagent with the proteins was studied by UV-Vis, fluorescence spectroscopic methods and docking description. PMA-SUC was found to bind to lysozyme and avidin with binding constants (K ) of 2.4×10 and 6.7×10 (M ), respectively. The fluorescence intensity of PMA-SUC decreased with increasing concentration of both proteins. Quenching of PMA-SUC fluorescence, in the absence and presence of the protein by an electron acceptor (Hexaamminecobalt(III) chloride, Co(NH ) Cl ) showed no significant changes in the K values (Stern-Volmer quenching constant), indicating that PMA-SUC bound to the hydrophilic sites or near the surface of the proteins. Irradiation of protein-PMA-SUC mixture, at 342nm for a period of time, in the presence of Co(NH ) Cl as an electron acceptor, resulted in the cleavage of both proteins with high specificity. Binding mechanisms were studied using Molecular docking method. Molecular docking study indicated the position of PMA-SUC upon binding to the proteins by hydrogen bonding interaction with donor-acceptor within the distance of less than 5Å in the minimum of binding free energy. The docking results have supported the results obtained from the spectroscopic methods and cleavage studies. [Mh] Termos MeSH primário: Avidina/metabolismo Muramidase/metabolismo Pirenos/química Succinatos/química [Mh] Termos MeSH secundário: Animais Avidina/química Sítios de Ligação Galinhas Ligações de Hidrogênio Simulação de Acoplamento Molecular Muramidase/química Fotólise/efeitos da radiação Ligação Proteica Estrutura Terciária de Proteína Pirenos/síntese química Pirenos/metabolismo Espectrometria de Fluorescência Espectrofotometria Ultravioleta Succinatos/síntese química Succinatos/metabolismo Raios Ultravioleta [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Pyrenes); 0 (Succinates); 0 (succinic acid-1(1-pyrene)methylamide); 1405-69-2 (Avidin); 9E0T7WFW93 (pyrene); EC 3.2.1.17 (Muramidase) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171006 [Lr] Data última revisão: 171006 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170530 [St] Status: MEDLINE

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[PMID]: 28444248 [Au] Autor: Sakamoto Y; Kikuchi K; Umeda K; Nakanishi H [Ad] Endereço: Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto 860-8556, Japan. [Ti] Título: Effects of various spacers between biotin and the phospholipid headgroup on immobilization and sedimentation of biotinylated phospholipid-containing liposomes facilitated by avidin-biotin interactions. [So] Source: J Biochem;162(3):221-226, 2017 Sep 01. [Is] ISSN: 1756-2651 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Immobilization and sedimentation of liposomes (lipid vesicles) are used in liposome-protein binding assays, facilitated by avidin/streptavidin/NeutrAvidin and biotinylated phospholipid-containing liposomes. Here, we examined the effects of three spacers [six-carbon (X), polyethylene glycol (PEG) 180 (molecular weight 180) and PEG2000 (molecular weight 2,000)] between biotin and the phospholipid headgroup on the immobilization and sedimentation of small unilamellar liposomes/vesicles (SUVs). PEG180 and PEG2000 showed more efficient immobilization of biotinylated SUVs on NeutrAvidin-coated plates than X, but X and PEG180 showed more efficient sedimentation of biotinylated SUVs upon NeutrAvidin addition than PEG2000. Thus, the most appropriate spacers differed between immobilization and sedimentation. A spacer for biotinylated SUVs must be selected according to the particular liposome-protein binding assays examined. [Mh] Termos MeSH primário: Avidina/química Biotina/química Lipossomos/química Fosfolipídeos/química [Mh] Termos MeSH secundário: Estrutura Molecular Fosfatidiletanolaminas/química Polietilenoglicóis/química [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Liposomes); 0 (Phosphatidylethanolamines); 0 (Phospholipids); 1405-69-2 (Avidin); 30IQX730WE (Polyethylene Glycols); 39382-08-6 (phosphatidylethanolamine); 6SO6U10H04 (Biotin) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171013 [Lr] Data última revisão: 171013 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170427 [St] Status: MEDLINE [do] DOI: 10.1093/jb/mvx016

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[PMID]: 28442904 [Au] Autor: Jurek PM; Zablocki K; Wasko U; Mazurek MP; Otlewski J; Jelen F [Ad] Endereço: Department of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Poland. [Ti] Título: Anti-FGFR1 aptamer-tagged superparamagnetic conjugates for anticancer hyperthermia therapy. [So] Source: Int J Nanomedicine;12:2941-2950, 2017. [Is] ISSN: 1178-2013 [Cp] País de publicação: New Zealand [La] Idioma: eng [Ab] Resumo: Compounds that recognize and strongly bind to molecular targets are one of the cornerstones of modern pharmaceutics. Work has been ongoing for the past 25 years on the therapeutic use of aptamers, nucleic acid molecules, whose three-dimensional structure is the result of interactions between complementary base pairs. The aptamers selection methods allow the oligonucleotides which bind the molecular target in its native environment to be quickly isolated from a large library of random oligonucleotides. The possibilities presented for aptamers in the field of targeted therapy require the application of effective carriers to counter the renal clearance effect and/or functional cargo to exert therapeutic action if the aptamer is only used as a targeting moiety. Lately, a material gaining ground in biomedical research is iron oxide particles, which exhibit a superparamagnetic characteristic at nanoscale levels. This allows the iron oxide nanoparticles to convert external magnetic energy into heat, a mechanism known as hyperthermy, and efficiently supports conventional oncological treatment. In this study, we describe an experimentally confirmed functional model of targeted anticancer hyperthermia therapy. Using the systematic evolution of ligands by exponential enrichment technique, we selected a DNA aptamer that specifically binds to the extracellular domain of recombinant fibroblast growth factor receptor type-1 (FGFR1) with a nanomolar dissociation constant. The chosen target plays an important role in many crucial cellular processes and is also considered a candidate protein that is involved in tumor initiation, survival and progression. Next, we combined the selected aptamer with iron oxide nanoparticles to produce aptamer superparamagnetic conjugates (ASCs). Finally, we found that targeted ASCs selectively destroy FGFR1-overexpressing human osteosarcoma cells U2OS upon magnetic field irradiation. [Mh] Termos MeSH primário: Antineoplásicos/farmacologia Aptâmeros de Nucleotídeos/farmacologia Hipertermia Induzida/métodos Nanopartículas de Magnetita/química Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/antagonistas & inibidores [Mh] Termos MeSH secundário: Antineoplásicos/química Aptâmeros de Nucleotídeos/química Aptâmeros de Nucleotídeos/metabolismo Avidina/química Linhagem Celular Tumoral Ensaios de Seleção de Medicamentos Antitumorais/métodos Óxido Ferroso-Férrico/química Seres Humanos Ligantes Terapia de Campo Magnético/métodos Terapia de Alvo Molecular Neoplasias/terapia Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antineoplastic Agents); 0 (Aptamers, Nucleotide); 0 (Ligands); 0 (Magnetite Nanoparticles); 1405-69-2 (Avidin); EC 2.7.10.1 (FGFR1 protein, human); EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1); XM0M87F357 (Ferrosoferric Oxide) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170814 [Lr] Data última revisão: 170814 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170427 [St] Status: MEDLINE [do] DOI: 10.2147/IJN.S125231

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[PMID]: 28355874 [Au] Autor: Lohse J; Swier LJYM; Oudshoorn RC; Médard G; Kuster B; Slotboom DJ; Witte MD [Ad] Endereço: Chemical Biology II, Stratingh Institute for Chemistry, University of Groningen , Nijenborgh 7, 9747 AG Groningen, The Netherlands. [Ti] Título: Targeted Diazotransfer Reagents Enable Selective Modification of Proteins with Azides. [So] Source: Bioconjug Chem;28(4):913-917, 2017 Apr 19. [Is] ISSN: 1520-4812 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: In chemical biology, azides are used to chemically manipulate target structures in a bioorthogonal manner for a plethora of applications ranging from target identification to the synthesis of homogeneously modified protein conjugates. While a variety of methods have been established to introduce the azido group into recombinant proteins, a method that directly converts specific amino groups in endogenous proteins is lacking. Here, we report the first biotin-tethered diazotransfer reagent DtBio and demonstrate that it selectively modifies the model proteins streptavidin and avidin and the membrane protein BioY on cell surface. The reagent converts amines in the proximity of the binding pocket to azides and leaves the remaining amino groups in streptavidin untouched. Reagents of this novel class will find use in target identification as well as the selective functionalization and bioorthogonal protection of proteins. [Mh] Termos MeSH primário: Avidina/química Azidas/química Proteínas de Bactérias/química Biotina/química Escherichia coli/química Lactococcus lactis/química Estreptavidina/química [Mh] Termos MeSH secundário: Alquinos/química Compostos de Boro/química Modelos Moleculares [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene); 0 (Alkynes); 0 (Azides); 0 (Bacterial Proteins); 0 (Boron Compounds); 1405-69-2 (Avidin); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170502 [Lr] Data última revisão: 170502 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170331 [St] Status: MEDLINE [do] DOI: 10.1021/acs.bioconjchem.7b00110

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