Base de dados : MEDLINE
Pesquisa : D12.644.456 [Categoria DeCS]
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  1 / 43337 MEDLINE  
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[PMID]:29220564
[Au] Autor:Benhaberou-Brun D
[Ti] Título:Cancer de la prostate. Les précautions liées à l'injection du dégarélix..
[So] Source:Perspect Infirm;14(3):52, 2017 May-Jun.
[Is] ISSN:1708-1890
[Cp] País de publicação:Canada
[La] Idioma:fre
[Mh] Termos MeSH primário: Oligopeptídeos/administração & dosagem
Neoplasias da Próstata/tratamento farmacológico
[Mh] Termos MeSH secundário: Seres Humanos
Injeções Subcutâneas/efeitos adversos
Injeções Subcutâneas/métodos
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligopeptides); 0 (acetyl-2-naphthylalanyl-3-chlorophenylalanyl-1-oxohexadecyl-seryl-4-aminophenylalanyl(hydroorotyl)-4-aminophenylalanyl(carbamoyl)-leucyl-ILys-prolyl-alaninamide)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:N
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


  2 / 43337 MEDLINE  
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[PMID]:28465342
[Au] Autor:Stefanova D; Raychev A; Arezes J; Ruchala P; Gabayan V; Skurnik M; Dillon BJ; Horwitz MA; Ganz T; Bulut Y; Nemeth E
[Ad] Endereço:Molecular, Cellular, and Integrative Physiology Graduate Program and.
[Ti] Título:Endogenous hepcidin and its agonist mediate resistance to selected infections by clearing non-transferrin-bound iron.
[So] Source:Blood;130(3):245-257, 2017 07 20.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The iron-regulatory hormone hepcidin is induced early in infection, causing iron sequestration in macrophages and decreased plasma iron; this is proposed to limit the replication of extracellular microbes, but could also promote infection with macrophage-tropic pathogens. The mechanisms by which hepcidin and hypoferremia modulate host defense, and the spectrum of microbes affected, are poorly understood. Using mouse models, we show that hepcidin was selectively protective against siderophilic extracellular pathogens ( O9) by controlling non-transferrin-bound iron (NTBI) rather than iron-transferrin concentration. NTBI promoted the rapid growth of siderophilic but not nonsiderophilic bacteria in mice with either genetic or iatrogenic iron overload and in human plasma. Hepcidin or iron loading did not affect other key components of innate immunity, did not indiscriminately promote intracellular infections ( ), and had no effect on extracellular nonsiderophilic O8 or Hepcidin analogs may be useful for treatment of siderophilic infections.
[Mh] Termos MeSH primário: Infecções Relacionadas a Cateter/imunologia
Hemocromatose/imunologia
Hepcidinas/imunologia
Sobrecarga de Ferro/imunologia
Ferro/metabolismo
Infecções Estafilocócicas/imunologia
[Mh] Termos MeSH secundário: Animais
Ligação Competitiva
Infecções Relacionadas a Cateter/metabolismo
Infecções Relacionadas a Cateter/microbiologia
Infecções Relacionadas a Cateter/mortalidade
Modelos Animais de Doenças
Resistência à Doença
Expressão Gênica
Hemocromatose/metabolismo
Hemocromatose/microbiologia
Hemocromatose/mortalidade
Hepcidinas/agonistas
Hepcidinas/deficiência
Hepcidinas/genética
Seres Humanos
Ferro/imunologia
Sobrecarga de Ferro/metabolismo
Sobrecarga de Ferro/microbiologia
Sobrecarga de Ferro/mortalidade
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/crescimento & desenvolvimento
Mycobacterium tuberculosis/metabolismo
Oligopeptídeos/farmacologia
Ligação Proteica
Infecções Estafilocócicas/metabolismo
Infecções Estafilocócicas/microbiologia
Infecções Estafilocócicas/mortalidade
Staphylococcus aureus
Análise de Sobrevida
Transferrina/genética
Transferrina/metabolismo
Yersinia enterocolitica/efeitos dos fármacos
Yersinia enterocolitica/crescimento & desenvolvimento
Yersinia enterocolitica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hamp1 protein, mouse); 0 (Hepcidins); 0 (Oligopeptides); 0 (Transferrin); E1UOL152H7 (Iron)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-03-772715


  3 / 43337 MEDLINE  
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[PMID]:28451782
[Au] Autor:Orosz Á; Bosze S; Mezo G; Szabó I; Herényi L; Csík G
[Ad] Endereço:Institute of Biophysics and Radiation Biology, Semmelweis University, POB 263, Budapest, 1444, Hungary.
[Ti] Título:Oligo- and polypeptide conjugates of cationic porphyrins: binding, cellular uptake, and cellular localization.
[So] Source:Amino Acids;49(7):1263-1276, 2017 07.
[Is] ISSN:1438-2199
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Recently, we have characterized the DNA and nucleoprotein (NP) binding of bis(4-N-methylpyridyl)-15,20-di(4-carboxyphenyl)porphyrin (BMPCP) and meso-tri(4-N-methylpyridyl)-mono(4-carboxyphenyl)porphyrin (TMPCP) and their tetrapeptide conjugates (BMPCP-4P and TMPCP-4P, respectively). In this work, we investigated the interaction of TMPCP conjugated to the tetrapeptide branches of branched chain polymeric polypeptide with poly-L-lysine backbone (AK) with DNA or NP using spectroscopic methods. Analysis of absorption spectra revealed the external binding but no intercalation of TMPCP-AK to DNA. There was no evidence for the interaction between TMPCP-AK and encapsidated DNA. Furthermore, we examined the cellular uptake of BMPCP and TMPCP and their tetra- or polypeptide conjugates by flow cytometry and analyzed how charge, size, and structure of the compounds affect their incorporation. In comparison, liposomal association constants of these derivatives were determined. BMPCP-4P accumulated the most, and porphyrins with two positive charges (BMPCP and BMPCP-4P ) showed better accumulation than the tri-cationic TMPCP or TMPCP-4P. Cellular uptake of polycationic TMPCP-AK was significantly lower than that of the free or tetrapeptide conjugated derivatives. The subcellular localization of all the five compounds was investigated in co-localization studies by confocal microscopy with special attention to their nuclear localization. Neither free nor conjugated BMPCP or TMPCP was co-localized with nuclear marker. Instead, these derivatives showed co-localization with lysosomal and mitochondrial fluorescent probes. TMPCP-AK conjugate had different localization patterns appearing mainly in mitochondria and cytoplasmic vesicles. Our results may contribute to the further design of DNA-targeting porphyrin-based constructs.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
DNA/metabolismo
Oligopeptídeos
Porfirinas
[Mh] Termos MeSH secundário: Células HL-60
Seres Humanos
Oligopeptídeos/síntese química
Oligopeptídeos/química
Oligopeptídeos/farmacocinética
Oligopeptídeos/farmacologia
Porfirinas/química
Porfirinas/farmacocinética
Porfirinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligopeptides); 0 (Porphyrins); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1007/s00726-017-2428-z


  4 / 43337 MEDLINE  
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[PMID]:29291444
[Au] Autor:Khodadust F; Ahmadpour S; Aligholikhamseh N; Abedi SM; Hosseinimehr SJ
[Ad] Endereço:Department of Radiopharmacy, Faculty of Pharmacy, Mazandaran University of Medical Sciences, Sari, Iran.
[Ti] Título:An improved Tc-HYNIC-(Ser) -LTVSPWY peptide with EDDA/tricine as co-ligands for targeting and imaging of HER2 overexpression tumor.
[So] Source:Eur J Med Chem;144:767-773, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Overexpression of human epidermal receptor 2 (HER2) has given the opportunity for targeting and delivering of imaging radiotracers. The aim of this study was to evaluate the Tc-HYNIC-(EDDA/tricine)-(Ser) -LTVSPWY peptide for tumor targeting and imaging of tumor with overexpression of HER2. The HYNIC-(Ser) -LTVSPWY was labeled with Tc in presence of EDDA/tricine mixture as co-ligands. The in vitro and in vivo studies of this radiolabeled peptide were performed for cellular specific binding and tumor targeting. The high radiochemical purity of Tc-HYNIC (EDDA/tricine)-(Ser) -LTVSPWY was obtained to be 99%. It exhibited high stability in normal saline and human serum. In HER2 binding affinity study, a significant reduction in uptake of radiolabeled peptide (7.7 fold) was observed by blocking SKOV-3 cells receptors with unlabeled peptide. The K and B values for this radiolabeled peptide were determined as 3.3 ±â€¯1.0 nM and 2.9 ±â€¯0.3 × 10 CPM/pMol, respectively. Biodistribution study revealed tumor to blood and tumor to muscle ratios about 6.9 and 4 respectively after 4 h. Tumor imaging by gamma camera demonstrated considerable high contrast tumor uptake. This developed Tc-HYNIC-(Ser) -LTVSPWY peptide selectively targeted on HER2 tumor and exhibited a high target uptake combined with acceptable low background activity for tumor imaging in mice. The results of this study and its comparison with another study showed that Tc-HYNIC-(EDDA/tricine)-(Ser) -LTVSPWY is much better than previously reported radiolabeled peptide as Tc-CSSS-LTVSPWY for HER2 overexpression tumor targeting and imaging.
[Mh] Termos MeSH primário: Glicina/análogos & derivados
Neoplasias/diagnóstico
Oligopeptídeos/farmacocinética
Compostos de Organotecnécio/farmacocinética
Receptor ErbB-2/biossíntese
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Relação Dose-Resposta a Droga
Feminino
Glicina/química
Glicina/farmacocinética
Seres Humanos
Ligantes
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Nus
Estrutura Molecular
Neoplasias/metabolismo
Neoplasias Experimentais/diagnóstico
Neoplasias Experimentais/metabolismo
Oligopeptídeos/síntese química
Oligopeptídeos/química
Compostos de Organotecnécio/síntese química
Compostos de Organotecnécio/química
Relação Estrutura-Atividade
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 ((99m)Tc-HYNIC-(Ser)3-LTVSPWY); 0 (Ligands); 0 (Oligopeptides); 0 (Organotechnetium Compounds); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); TE7660XO1C (Glycine); W12LH4V8V3 (tricine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180102
[St] Status:MEDLINE


  5 / 43337 MEDLINE  
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[PMID]:27771849
[Au] Autor:Lapphanichayakool P; Sutheerawattananonda M; Limpeanchob N
[Ad] Endereço:Department of Pharmacy Practice, Faculty of Pharmaceutical Science, Center of Excellence for Innovation in Chemistry, Naresuan University, Phitsanulok, 65000, Thailand.
[Ti] Título:Hypocholesterolemic effect of sericin-derived oligopeptides in high-cholesterol fed rats.
[So] Source:J Nat Med;71(1):208-215, 2017 Jan.
[Is] ISSN:1861-0293
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The beneficial effect of cholesterol-lowering proteins and/or peptides derived from various dietary sources is continuously reported. A non-dietary protein from silk cocoon, sericin, has also demonstrated cholesterol-lowering activity. A sericin hydrolysate prepared by enzymatic hydrolysis was also expected to posses this effect. The present study was aimed at investigating the cholesterol-lowering effect of sericin peptides, so called "sericin-derived oligopeptides" (SDO) both in vivo and in vitro. The results showed that SDO at all three doses tested (10 mg kg day , 50 mg kg day , and 200 mg kg day ) suppressed serum total and non-HDL cholesterol levels in rats fed a high-cholesterol diet. Triglyceride and HDL-cholesterol levels were not significantly changed among all groups. The fecal contents of bile acids and cholesterol did not differ among high-cholesterol fed rats. SDO dose-dependently reduced cholesterol solubility in lipid micelles, and inhibited cholesterol uptake in monolayer Caco-2 cells. SDO also effectively bound to all three types of bile salts including taurocholate, deoxytaurocholate, and glycodeoxycholate. Direct interaction with bile acids of SDO may disrupt micellar cholesterol solubility, and subsequently reduce the absorption of dietary cholesterol in intestines. Taking all data together, SDO or sericin peptides exhibit a beneficial effect on blood cholesterol levels and could be potentially used as a health-promoting dietary supplement or nutraceutical product.
[Mh] Termos MeSH primário: Colesterol/sangue
Hipercolesterolemia/tratamento farmacológico
Sericinas/uso terapêutico
Triglicerídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CACO-2
Modelos Animais de Doenças
Seres Humanos
Masculino
Oligopeptídeos
Ratos
Ratos Sprague-Dawley
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligopeptides); 0 (Sericins); 0 (Triglycerides); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1007/s11418-016-1050-9


  6 / 43337 MEDLINE  
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[PMID]:29190078
[Au] Autor:Gonzalez P; Vileno B; Bossak K; El Khoury Y; Hellwig P; Bal W; Hureau C; Faller P
[Ad] Endereço:Institut de Chimie, UMR 7177, CNRS, Université de Strasbourg , 4 rue Blaise Pascal 67000, Strasbourg, France.
[Ti] Título:Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His.
[So] Source:Inorg Chem;56(24):14870-14879, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peptides and proteins with the N-terminal motifs NH -Xxx-His and NH -Xxx-Zzz-His form well-established Cu(II) complexes. The canonical peptides are Gly-His-Lys and Asp-Ala-His-Lys (from the wound healing factor and human serum albumin, respectively). Cu(II) is bound to NH -Xxx-His via three nitrogens from the peptide and an external ligand in the equatorial plane (called 3N form here). In contrast, Cu(II) is bound to NH -Xxx-Zzz-His via four nitrogens from the peptide in the equatorial plane (called 4N form here). These two motifs are not mutually exclusive, as the peptides with the sequence NH -Xxx-His-His contain both of them. However, this chimera has never been fully explored. In this work, we use a multispectroscopic approach to analyze the Cu(II) binding to the chimeric peptide Ala-His-His (AHH). AHH is capable of forming the 3N- and 4N-type complexes in a pH dependent manner. The 3N form predominates at pH ∼ 4-6.5 and the 4N form at ∼ pH 6.5-10. NMR experiments showed that at pH 8.5, where Cu(II) is almost exclusively bound in the 4N form, the Cu(II)-exchange between AHH or the amidated AHH-NH is fast, in comparison to the nonchimeric 4N form (AAH). Together, the results show that the chimeric AHH can access both Cu(II) coordination types, that minor changes in the second (or further) coordination sphere can impact considerably the equilibrium between the forms, and that Cu kinetic exchange is fast even when Cu-AHH is mainly in the 4N form.
[Mh] Termos MeSH primário: Complexos de Coordenação/química
Cobre/química
Oligopeptídeos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dimerização
Espectroscopia de Ressonância de Spin Eletrônica
Concentração de Íons de Hidrogênio
Cinética
Espectroscopia de Ressonância Magnética
Potenciometria
Conformação Proteica
Proteínas/química
Espectroscopia de Infravermelho com Transformada de Fourier
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ala-His-His); 0 (Coordination Complexes); 0 (Oligopeptides); 0 (Proteins); 789U1901C5 (Copper)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b01996


  7 / 43337 MEDLINE  
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[PMID]:29340380
[Au] Autor:Fang Z; Wang J; Zhu S; Yang X; Jia Y; Sun Q; Guan S
[Ad] Endereço:School of Materials Science and Engineering, Zhengzhou University, Zhengzhou 450001, China. skguan@zzu.edu.cn.
[Ti] Título:A DFT study of the adsorption of short peptides on Mg and Mg-based alloy surfaces.
[So] Source:Phys Chem Chem Phys;20(5):3602-3607, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Adsorption of short peptides, including three dipeptides: arginine-glycine (Arg-Gly), glycine-aspartic acid (Gly-Asp), arginine-aspartic acid (Arg-Asp), and one tripeptide arginine-glycine-aspartic acid (RGD), on the surfaces of Mg and Mg alloys (Mg-Zn, Mg-Y, and Mg-Nd), was studied using the first-principles calculations based on density functional theory (DFT), considering van der Waals (vdW) correction. The calculated adsorption energies (E ) of short peptides on the clean Mg(0001) surface are in the range of -1.73 to -2.80 eV per dipeptide, and -3.24 eV for RGD. The short peptides prefer to bond to Mg atoms at the surface by the O and N anions in their functional groups. For the clean Mg(0001) surface, the E of the short peptides are exclusively dominated by the number of functional groups binding to the surface. However, for the surface of the Mg-Zn alloy (1% Zn), the adsorption of the peptides is clearly enhanced (by about 0.3 eV per peptide) due to the enhanced N-Mg bond and the electrostatic interactions between the doped Zn at the surface and the backbone chains of the peptides. Furthermore, the attractive interactions are increased with the increase of doped Zn contents (up to 3%). In contrast, for the surfaces of Mg-Y (1% Y) and Mg-Nd (1% Nd) alloys, the adsorption of the peptides is slightly weakened compared to that on the clean Mg(0001) surfaces. Our results provide useful guidance in understanding the interactions between peptides and the Mg-based biomedical alloy surfaces at the atomic scale in the biomimetic coating fields.
[Mh] Termos MeSH primário: Ligas/química
Dipeptídeos/química
Magnésio/química
Oligopeptídeos/química
[Mh] Termos MeSH secundário: Adsorção
Dipeptídeos/metabolismo
Oligopeptídeos/metabolismo
Teoria Quântica
Eletricidade Estática
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alloys); 0 (Dipeptides); 0 (Oligopeptides); 78VO7F77PN (arginyl-glycyl-aspartic acid); I38ZP9992A (Magnesium)
[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:180118
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07431j


  8 / 43337 MEDLINE  
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[PMID]:29340378
[Au] Autor:Homayoon Z; Macaluso V; Martin-Somer A; Muniz MCNB; Borges I; Hase WL; Spezia R
[Ad] Endereço:Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061 USA. bill.hase@ttu.edu.
[Ti] Título:Chemical dynamics simulations of CID of peptide ions: comparisons between TIK(H ) and TLK(H ) fragmentation dynamics, and with thermal simulations.
[So] Source:Phys Chem Chem Phys;20(5):3614-3629, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gas phase unimolecular fragmentation of the two model doubly protonated tripeptides threonine-isoleucine-lysine (TIK) and threonine-leucine-lysine (TLK) is studied using chemical dynamics simulations. Attention is focused on different aspects of collision induced dissociation (CID): fragmentation pathways, energy transfer, theoretical mass spectra, fragmentation mechanisms, and the possibility of distinguishing isoleucine (I) and leucine (L). Furthermore, discussion is given regarding the differences between single collision CID activation, which results from a localized impact between the ions and a colliding molecule N , and previous thermal activation simulation results; Z. Homayoon, S. Pratihar, E. Dratz, R. Snider, R. Spezia, G. L. Barnes, V. Macaluso, A. Martin-Somer and W. L. Hase, J. Phys. Chem. A, 2016, 120, 8211-8227. Upon thermal activation unimolecular fragmentation is statistical and in accord with RRKM unimolecular rate theory. Simulations show that in collisional activation some non-statistical fragmentation occurs, including shattering, which is not present when the ions dissociate statistically. Products formed by non-statistical shattering mechanisms may be related to characteristic mass spectrometry peaks which distinguish the two isomers I and L.
[Mh] Termos MeSH primário: Oligopeptídeos/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Transferência de Energia
Íons/química
Estrutura Secundária de Proteína
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ions); 0 (Oligopeptides)
[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:180118
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06818b


  9 / 43337 MEDLINE  
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[PMID]:28449309
[Au] Autor:Zanella S; Angerani S; Pina A; López Rivas P; Giannini C; Panzeri S; Arosio D; Caruso M; Gasparri F; Fraietta I; Albanese C; Marsiglio A; Pignataro L; Belvisi L; Piarulli U; Gennari C
[Ad] Endereço:Dipartimento di Chimica, Università degli Studi di Milano, Via C. Golgi 19, 20133, Milano, Italy.
[Ti] Título:Tumor Targeting with an isoDGR-Drug Conjugate.
[So] Source:Chemistry;23(33):7910-7914, 2017 Jun 12.
[Is] ISSN:1521-3765
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Herein we report the first example of an isoDGR-drug conjugate (2), designed to release paclitaxel selectively within cancer cells expressing integrin α ß . Conjugate 2 was synthesized by connecting the isoDGR peptidomimetic 5 with paclitaxel via the lysosomally cleavable Val-Ala dipeptide linker. Conjugate 2 displayed a low nanomolar affinity for the purified integrin α ß receptor (IC =11.0 nm). The tumor targeting ability of conjugate 2 was assessed in vitro in anti-proliferative assays on two isogenic cancer cell lines characterized by different integrin α ß expression: human glioblastoma U87 (α ß +) and U87 ß -KO (α ß -). The isoDGR-PTX conjugate 2 displayed a remarkable targeting index (TI=9.9), especially when compared to the strictly related RGD-PTX conjugate 4 (TI=2.4).
[Mh] Termos MeSH primário: Oligopeptídeos/química
Paclitaxel/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Seres Humanos
Concentração Inibidora 50
Integrina alfaVbeta3/antagonistas & inibidores
Integrina alfaVbeta3/genética
Integrina alfaVbeta3/metabolismo
Peptidomiméticos/química
Peptidomiméticos/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alphaVbeta3); 0 (Oligopeptides); 0 (Peptidomimetics); 78VO7F77PN (arginyl-glycyl-aspartic acid); P88XT4IS4D (Paclitaxel)
[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:170428
[St] Status:MEDLINE
[do] DOI:10.1002/chem.201701844


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[PMID]:29370189
[Au] Autor:Gallery M; Zhang J; Bradley DP; Brauer P; Cvet D; Estevam J; Danaee H; Greenfield E; Li P; Manfredi M; Loke HK; Rabino C; Stringer B; Williamson M; Wyant T; Yang J; Zhu Q; Abu-Yousif A; Veiby OP
[Ad] Endereço:Molecular & Cellular Oncology, Millennium Pharmaceuticals, Inc., a wholly owned subsidiary of Takeda Pharmaceutical Company Limited, Cambridge, MA, United States of America.
[Ti] Título:A monomethyl auristatin E-conjugated antibody to guanylyl cyclase C is cytotoxic to target-expressing cells in vitro and in vivo.
[So] Source:PLoS One;13(1):e0191046, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Guanylyl cyclase C (GCC) is a cell-surface protein that is expressed by normal intestinal epithelial cells, more than 95% of metastatic colorectal cancers (mCRC), and the majority of gastric and pancreatic cancers. Due to strict apical localization, systemically delivered GCC-targeting agents should not reach GCC in normal intestinal tissue, while accessing antigen in tumor. We generated an investigational antibody-drug conjugate (TAK-264, formerly MLN0264) comprising a fully human anti-GCC monoclonal antibody conjugated to monomethyl auristatin E via a protease-cleavable peptide linker. TAK-264 specifically bound, was internalized by, and killed GCC-expressing cells in vitro in an antigen-density-dependent manner. In GCC-expressing xenograft models with similar GCC expression levels/patterns observed in human mCRC samples, TAK-264 induced cell death, leading to tumor regressions and long-term tumor growth inhibition. TAK-264 antitumor activity was generally antigen-density-dependent, although some GCC-expressing tumors were refractory to TAK-264-targeted high local concentrations of payload. These data support further evaluation of TAK-264 in the treatment of GCC-expressing tumors.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Imunoconjugados/farmacologia
Oligopeptídeos/metabolismo
Receptores de Enterotoxina/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/metabolismo
Western Blotting
Neoplasias Colorretais/enzimologia
Neoplasias Colorretais/patologia
Feminino
Células HEK293
Seres Humanos
Mucosa Intestinal/enzimologia
Camundongos
Camundongos SCID
Receptores de Enterotoxina/genética
Receptores de Enterotoxina/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Immunoconjugates); 0 (Oligopeptides); 0 (indusatumab); EC 4.6.1.2 (Receptors, Enterotoxin); V7I58RC5EJ (monomethyl auristatin E)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191046



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