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  1 / 12454 MEDLINE  
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[PMID]:29324341
[Au] Autor:Maiti S; Paira P
[Ad] Endereço:Department of Chemistry, School of Advanced Sciences, VIT University, Vellore 632014, Tamilnadu, India.
[Ti] Título:Biotin conjugated organic molecules and proteins for cancer therapy: A review.
[So] Source:Eur J Med Chem;145:206-223, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The main transporter for biotin is sodium dependent multivitamin transporter (SMVT), which is overexpressed in various aggressive cancer cell lines such as ovarian (OV 2008, ID8), leukemia (L1210FR), mastocytoma (P815), colon (Colo-26), breast (4T1, JC, MMT06056), renal (RENCA, RD0995), and lung (M109) cancer cell lines. Furthermore, its overexpression was found higher to that of folate receptor. Therefore, biotin demand in the rapidly growing tumors is higher than normal tissues. Several biotin conjugated organic molecules has been reported here for selective delivery of the drug in cancer cell. Biotin conjugated molecules are showing higher fold of cytotoxicity in biotin positive cancer cell lines than the normal cell. Nanoparticles and polymer surface modified drugs and biotin mediated cancer theranostic strategy was highlighted in this review. The cytotoxicity and selectivity of the drug in cancer cells has enhanced after biotin conjugation.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Biotina/metabolismo
Neoplasias/tratamento farmacológico
Compostos Orgânicos/farmacologia
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos/química
Biotina/química
Proliferação Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Seres Humanos
Estrutura Molecular
Neoplasias/patologia
Compostos Orgânicos/química
Proteínas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Organic Chemicals); 0 (Proteins); 6SO6U10H04 (Biotin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


  2 / 12454 MEDLINE  
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[PMID]:29371614
[Au] Autor:Sreekanth KV; Sreejith S; Han S; Mishra A; Chen X; Sun H; Lim CT; Singh R
[Ad] Endereço:Division of Physics and Applied Physics, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Singapore.
[Ti] Título:Biosensing with the singular phase of an ultrathin metal-dielectric nanophotonic cavity.
[So] Source:Nat Commun;9(1):369, 2018 01 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The concept of point of darkness has received much attention for biosensing based on phase-sensitive detection and perfect absorption of light. The maximum phase change is possible at the point of darkness where the reflection is almost zero. To date, this has been experimentally realized using different material systems through the concept of topological darkness. However, complex nanopatterning techniques are required to realize topological darkness. Here, we report an approach to realize perfect absorption and extreme phase singularity using a simple metal-dielectric multilayer thin-film stack. The multilayer stack works on the principle of an asymmetric Fabry-Perot cavity and shows an abrupt phase change at the reflectionless point due to the presence of a highly absorbing ultrathin film of germanium in the stack. In the proof-of-concept phase-sensitive biosensing experiments, we functionalize the film surface with an ultrathin layer of biotin-thiol to capture streptavidin at a low concentration of 1 pM.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Metais/química
[Mh] Termos MeSH secundário: Biotina/química
Estreptavidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Metals); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02860-6


  3 / 12454 MEDLINE  
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[PMID]:29360877
[Au] Autor:Verma V; Kaur C; Grover P; Gupta A; Chaudhary VK
[Ad] Endereço:Centre for Innovation in Infectious Disease Research, Education and Training (CIIDRET), University of Delhi South Campus, New Delhi, India.
[Ti] Título:Biotin-tagged proteins: Reagents for efficient ELISA-based serodiagnosis and phage display-based affinity selection.
[So] Source:PLoS One;13(1):e0191315, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The high-affinity interaction between biotin and streptavidin has opened avenues for using recombinant proteins with site-specific biotinylation to achieve efficient and directional immobilization. The site-specific biotinylation of proteins carrying a 15 amino acid long Biotin Acceptor Peptide tag (BAP; also known as AviTag) is effected on a specific lysine either by co-expressing the E. coli BirA enzyme in vivo or by using purified recombinant E. coli BirA enzyme in the presence of ATP and biotin in vitro. In this paper, we have designed a T7 promoter-lac operator-based expression vector for rapid and efficient cloning, and high-level cytosolic expression of proteins carrying a C-terminal BAP tag in E. coli with TEV protease cleavable N-terminal deca-histidine tag, useful for initial purification. Furthermore, a robust three-step purification pipeline integrated with well-optimized protocols for TEV protease-based H10 tag removal, and recombinant BirA enzyme-based site-specific in vitro biotinylation is described to obtain highly pure biotinylated proteins. Most importantly, the paper demonstrates superior sensitivities in indirect ELISA with directional and efficient immobilization of biotin-tagged proteins on streptavidin-coated surfaces in comparison to passive immobilization. The use of biotin-tagged proteins through specific immobilization also allows more efficient selection of binders from a phage-displayed naïve antibody library. In addition, for both these applications, specific immobilization requires much less amount of protein as compared to passive immobilization and can be easily multiplexed. The simplified strategy described here for the production of highly pure biotin-tagged proteins will find use in numerous applications, including those, which may require immobilization of multiple proteins simultaneously on a solid surface.
[Mh] Termos MeSH primário: Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/metabolismo
Biotina/metabolismo
Ensaio de Imunoadsorção Enzimática/métodos
Biblioteca de Peptídeos
Testes Sorológicos/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biotinilação
Carbono-Nitrogênio Ligases/metabolismo
Clonagem Molecular
Citosol/metabolismo
Escherichia coli/citologia
Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Vetores Genéticos/genética
Indicadores e Reagentes/metabolismo
Mycobacterium tuberculosis/genética
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Indicators and Reagents); 0 (Peptide Library); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191315


  4 / 12454 MEDLINE  
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[PMID]:28470616
[Au] Autor:Gräslund S; Savitsky P; Müller-Knapp S
[Ad] Endereço:Structural Genomics Consortium, Department of Biochemistry and Biophysics, Karolinska Institutet, Tomtebodavägen 23a, Gamma:6, 171 65, Solna, Sweden. susanne.graslund@ki.se.
[Ti] Título:In Vivo Biotinylation of Antigens in E. coli.
[So] Source:Methods Mol Biol;1586:337-344, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Site-specific biotinylation of proteins is often the method of choice to enable efficient immobilization of a protein on a surface without interfering with protein folding. The tight interaction of biotin and streptavidin is frequently used to immobilize an antigen during phage display selections of binders. Here we describe a method of in vivo biotinylation of proteins during expression in E. coli, by tagging the protein with the short biotin acceptor peptide sequence, Avi tag, and co-expression of the E. coli biotin ligase (BirA) resulting in precise biotinylation of a specific lysine residue in the tag.
[Mh] Termos MeSH primário: Antígenos/química
Antígenos/genética
Escherichia coli/genética
Proteínas Imobilizadas/química
Proteínas Imobilizadas/genética
[Mh] Termos MeSH secundário: Animais
Biotina/química
Biotinilação
Carbono-Nitrogênio Ligases/química
Carbono-Nitrogênio Ligases/genética
Clonagem Molecular/métodos
Escherichia coli/química
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Expressão Gênica
Vetores Genéticos/genética
Seres Humanos
Proteínas Repressoras/química
Proteínas Repressoras/genética
Estreptavidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens); 0 (Escherichia coli Proteins); 0 (Immobilized Proteins); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_22


  5 / 12454 MEDLINE  
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[PMID]:27774548
[Au] Autor:Shi WJ; Lo PC; Zhao S; Wong RC; Wang Q; Fong WP; Ng DK
[Ad] Endereço:Department of Chemistry, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China. dkpn@cuhk.edu.hk.
[Ti] Título:A biotin-conjugated glutathione-responsive FRET-based fluorescent probe with a ferrocenyl BODIPY as the dark quencher.
[So] Source:Dalton Trans;45(44):17798-17806, 2016 Nov 28.
[Is] ISSN:1477-9234
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An efficient ferrocenyl BODIPY based dark quencher has been developed and employed to construct a FRET-based fluorescent probe that contains a biotin moiety as a potential directing ligand for cancer cells and a glutathione-cleavable disulfide linker connecting the quencher and a distyryl BODIPY fluorophore. This molecular probe is deactivated in the native form through FRET followed by intramolecular charge transfer due to the ferrocenyl unit. However, upon interaction with glutathione in phosphate buffered saline and inside cancer cells, the fluorescence emission is significantly increased due to detachment of the fluorophore from the quencher. As shown by flow cytometry, this probe also exhibits preferential uptake by the biotin-receptor-expressing A549 human lung adenocarcinoma epithelial cells over the Chinese hamster ovary CHO-K1 cells used as the negative control. On the basis that both biotin receptor and GSH level are often overexpressed or elevated in cancer cells, this dual functional fluorescent probe serves as a promising agent for cancer imaging.
[Mh] Termos MeSH primário: Biotina/química
Compostos de Boro/química
Corantes Fluorescentes/química
Glutationa/análise
[Mh] Termos MeSH secundário: Células A549
Animais
Células CHO
Cricetulus
Compostos Ferrosos/química
Transferência Ressonante de Energia de Fluorescência
Seres Humanos
Neoplasias/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene); 0 (Boron Compounds); 0 (Ferrous Compounds); 0 (Fluorescent Dyes); 6SO6U10H04 (Biotin); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  6 / 12454 MEDLINE  
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[PMID]:29206886
[Au] Autor:Sedlak SM; Bauer MS; Kluger C; Schendel LC; Milles LF; Pippig DA; Gaub HE
[Ad] Endereço:Lehrstuhl für Angewandte Physik and Center for NanoScience (CeNS), Ludwig-Maximilians-Universität München, Munich, Germany.
[Ti] Título:Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry.
[So] Source:PLoS One;12(12):e0188722, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The widely used interaction of the homotetramer streptavidin with the small molecule biotin has been intensively studied by force spectroscopy and has become a model system for receptor ligand interaction. However, streptavidin's tetravalency results in diverse force propagation pathways through the different binding interfaces. This multiplicity gives rise to polydisperse force spectroscopy data. Here, we present an engineered monovalent streptavidin tetramer with a single cysteine in its functional subunit that allows for site-specific immobilization of the molecule, orthogonal to biotin binding. Functionality of streptavidin and its binding properties for biotin remain unaffected. We thus created a stable and reliable molecular anchor with a unique high-affinity binding site for biotinylated molecules or nanoparticles, which we expect to be useful for many single-molecule applications. To characterize the mechanical properties of the bond between biotin and our monovalent streptavidin, we performed force spectroscopy experiments using an atomic force microscope. We were able to conduct measurements at the single-molecule level with 1:1-stoichiometry and a well-defined geometry, in which force exclusively propagates through a single subunit of the streptavidin tetramer. For different force loading rates, we obtained narrow force distributions of the bond rupture forces ranging from 200 pN at 1,500 pN/s to 230 pN at 110,000 pN/s. The data are in very good agreement with the standard Bell-Evans model with a single potential barrier at Δx0 = 0.38 nm and a zero-force off-rate koff,0 in the 10-6 s-1 range.
[Mh] Termos MeSH primário: Biotina/química
Estreptavidina/química
[Mh] Termos MeSH secundário: Calorimetria
Cisteína/química
Eletroforese em Gel de Poliacrilamida
Microscopia de Força Atômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188722


  7 / 12454 MEDLINE  
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[PMID]:28747322
[Au] Autor:Panchapakesan SSS; Ferguson ML; Hayden EJ; Chen X; Hoskins AA; Unrau PJ
[Ad] Endereço:Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
[Ti] Título:Ribonucleoprotein purification and characterization using RNA Mango.
[So] Source:RNA;23(10):1592-1599, 2017 10.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The characterization of RNA-protein complexes (RNPs) is a difficult but increasingly important problem in modern biology. By combining the compact RNA Mango aptamer with a fluorogenic thiazole orange desthiobiotin (TO1-Dtb or TO3-Dtb) ligand, we have created an RNA tagging system that simplifies the purification and subsequent characterization of endogenous RNPs. Mango-tagged RNP complexes can be immobilized on a streptavidin solid support and recovered in their native state by the addition of free biotin. Furthermore, Mango-based RNP purification can be adapted to different scales of RNP isolation ranging from pull-down assays to the isolation of large amounts of biochemically defined cellular RNPs. We have incorporated the Mango aptamer into the U1 small nuclear RNA (snRNA), shown that the Mango-snRNA is functional in cells, and used the aptamer to pull down a U1 snRNA-associated protein. To demonstrate large-scale isolation of RNPs, we purified and characterized bacterial RNA polymerase holoenzyme (HE) in complex with a Mango-containing 6S RNA. We were able to use the combination of a red-shifted TO3-Dtb ligand and eGFP-tagged HE to follow the binding and release of the 6S RNA by two-color native gel analysis as well as by single-molecule fluorescence cross-correlation spectroscopy. Together these experiments demonstrate how the Mango aptamer in conjunction with simple derivatives of its flurophore ligands enables the purification and characterization of endogenous cellular RNPs in vitro.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Bioquímica/métodos
Ribonucleoproteínas/isolamento & purificação
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Benzotiazóis/química
Biotina/análogos & derivados
Biotina/química
Proteínas de Fluorescência Verde/genética
Quinolinas/química
RNA Bacteriano/metabolismo
RNA Nuclear Pequeno/química
RNA não Traduzido/metabolismo
Ribonucleoproteínas/metabolismo
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (6S RNA); 0 (Aptamers, Nucleotide); 0 (Benzothiazoles); 0 (Quinolines); 0 (RNA, Bacterial); 0 (RNA, Small Nuclear); 0 (RNA, Untranslated); 0 (Ribonucleoproteins); 0 (U1 small nuclear RNA); 107091-89-4 (thiazole orange); 147336-22-9 (Green Fluorescent Proteins); 6SO6U10H04 (Biotin); 71U5JB52KS (desthiobiotin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1261/rna.062166.117


  8 / 12454 MEDLINE  
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[PMID]:27779387
[Au] Autor:Ngambenjawong C; Pineda JM; Pun SH
[Ad] Endereço:Department of Bioengineering and Molecular Engineering and Sciences Institute, University of Washington , Seattle, Washington 98195, United States.
[Ti] Título:Engineering an Affinity-Enhanced Peptide through Optimization of Cyclization Chemistry.
[So] Source:Bioconjug Chem;27(12):2854-2862, 2016 Dec 21.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peptide cyclization is a strategy used to improve stability and activity of peptides. The most commonly used cyclization method is disulfide bridge formation of cysteine-containing peptides, as is typically found in nature. Over the years, an increasing number of alternative chemistries for peptide cyclization with improved efficiency, kinetics, orthogonality, and stability have been reported. However, there has been less appreciation for the opportunity to fine-tune peptide activity via the diverse chemical entities introduced at the site of linkage by different cyclization strategies. Here, we demonstrate how cyclization optimization of an M2 "anti-inflammatory" macrophage-binding peptide (M2pep) resulted in a significant increase in binding affinity of the optimized analog to M2 macrophages while maintaining binding selectivity compared to M1 "pro-inflammatory" macrophages. In this study, we report synthesis and evaluation of four cyclic M2pep(RY) analogs with diverse cyclization strategies: (1) Asp-[amide]-Lys, (2) azido-Lys-[triazole(copper(I)-catalyzed alkyne-azide cycloaddition (CuAAC))]-propargyl-Gly, (3) Cys-[decafluorobiphenyl (DFBP)]-Cys, and (4) Cys-[decafluorobiphenyl sulfone (DFS)]-Cys, whereby the chemical entity or linker at the linkage site is shown in the square bracket and is between the residues involved in cyclization. These peptides are compared to a disulfide-cyclized M2pep(RY) that we previously reported as a serum-stable, affinity-enhanced analog to the original linear M2pep. DFBP-cyclized M2pep(RY) exhibits the highest binding activity to M2 macrophages with apparent dissociation constant (K ) about 2.03 µM compared to 36.3 µM for the original disulfide-cyclized M2pep(RY) and 220 µM for the original linear peptide. DFS-cyclized M2pep(RY) also binds more strongly than the original cyclized analog, whereas amide- and triazole-cyclized M2pep(RY) analogs bind less strongly. We verified that DFBP alone has negligible binding to M2 macrophages and the incorporation of diphenylalanine to the original sequence improves binding activity at the expense of solubility and increased toxicity. In conclusion, we report development of cyclic M2pep(RY) analogs with diverse cyclization strategies leading to the discovery of DFBP-cyclized M2pep(RY) with enhanced M2 macrophage-binding activity.
[Mh] Termos MeSH primário: Peptídeos/química
Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Azidas/química
Biotina/química
Técnicas de Química Sintética
Dicroísmo Circular
Macrófagos/metabolismo
Camundongos
Peptídeos/sangue
Peptídeos/síntese química
Engenharia de Proteínas/métodos
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azides); 0 (Peptides); 6SO6U10H04 (Biotin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171222
[Lr] Data última revisão:
171222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.6b00502


  9 / 12454 MEDLINE  
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[PMID]:29236641
[Au] Autor:Eichler FS; Swoboda KJ; Hunt AL; Cestari DM; Rapalino O
[Ad] Endereço:From the Departments of Neurology (F.S.E., K.J.S., A.L.H.) and Radiology (O.R.), Massachusetts General Hospital, the Departments of Neurology (F.S.E., K.J.S., A.L.H.), Ophthalmology (D.M.C.), and Radiology (O.R.), Harvard Medical School, and the Department of Ophthalmology, Massachusetts Eye and Ear
[Ti] Título:Case 38-2017. A 20-Year-Old Woman with Seizures and Progressive Dystonia.
[So] Source:N Engl J Med;377(24):2376-2385, 2017 Dec 14.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Doenças dos Gânglios da Base/diagnóstico
Distonia/etiologia
Proteínas de Membrana Transportadoras/genética
Mutação
Convulsões/etiologia
[Mh] Termos MeSH secundário: Doenças dos Gânglios da Base/complicações
Doenças dos Gânglios da Base/tratamento farmacológico
Doenças dos Gânglios da Base/genética
Biotina/uso terapêutico
Encéfalo/diagnóstico por imagem
Carbidopa/uso terapêutico
Diagnóstico Diferencial
Combinação de Medicamentos
Distonia/tratamento farmacológico
Feminino
Seres Humanos
Levodopa/uso terapêutico
Macula Lutea/patologia
Imagem por Ressonância Magnética
Erros Inatos do Metabolismo/diagnóstico
Nervo Óptico/patologia
Tiamina/uso terapêutico
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; CLINICAL CONFERENCE; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drug Combinations); 0 (Membrane Transport Proteins); 0 (SLC19A3 protein, human); 0 (carbidopa, levodopa drug combination); 46627O600J (Levodopa); 6SO6U10H04 (Biotin); MNX7R8C5VO (Carbidopa); X66NSO3N35 (Thiamine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMcpc1706109


  10 / 12454 MEDLINE  
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[PMID]:28986262
[Au] Autor:Cheah JS; Yamada S
[Ad] Endereço:Biomedical Engineering Department, University of California, Davis, United States.
[Ti] Título:A simple elution strategy for biotinylated proteins bound to streptavidin conjugated beads using excess biotin and heat.
[So] Source:Biochem Biophys Res Commun;493(4):1522-1527, 2017 Dec 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-protein interactions are the molecular basis of cell signaling. Recently, proximity based biotin identification (BioID) has emerged as an alternative approach to traditional co-immunoprecipitation. In this protocol, a mutant biotin ligase promiscuously labels proximal binding partners with biotin, and resulting biotinylated proteins are purified using streptavidin conjugated beads. This approach does not require preservation of protein complexes in vitro, making it an ideal approach to identify transient or weak protein complexes. However, due to the high affinity bond between streptavidin and biotin, elution of biotinylated proteins from streptavidin conjugated beads requires harsh denaturing conditions, which are often incompatible with downstream processing. To effectively release biotinylated proteins bound to streptavidin conjugated beads, we designed a series of experiments to determine optimal binding and elution conditions. Interestingly, the concentrations of SDS and IGEPAL-CA630 during the incubation with streptavidin conjugated beads were the key to effective elution of biotinylated proteins using excess biotin and heating. This protocol provides an alternative method to isolate biotinylated proteins from streptavidin conjugated beads that is suitable for further downstream analysis.
[Mh] Termos MeSH primário: Biotina/química
Proteínas/química
Proteínas/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Biotinilação
Western Blotting
Carbono-Nitrogênio Ligases/genética
Carbono-Nitrogênio Ligases/metabolismo
Cães
Eletroforese em Gel de Poliacrilamida
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Temperatura Alta
Imunoprecipitação
Células Madin Darby de Rim Canino
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Solubilidade
Estreptavidina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Proteins); 0 (Recombinant Proteins); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171008
[St] Status:MEDLINE



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