Base de dados : MEDLINE
Pesquisa : E05.196.867.151 [Categoria DeCS]
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  1 / 39711 MEDLINE  
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[PMID]:29346419
[Au] Autor:Holcomb J; Doughan M; Spellmon N; Lewis B; Perry E; Zhang Y; Nico L; Wan J; Chakravarthy S; Shang W; Miao Q; Stemmler T; Yang Z
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, United States of America.
[Ti] Título:SAXS analysis of a soluble cytosolic NgBR construct including extracellular and transmembrane domains.
[So] Source:PLoS One;13(1):e0191371, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Nogo-B receptor (NgBR) is involved in oncogenic Ras signaling through directly binding to farnesylated Ras. It recruits farnesylated Ras to the non-lipid-raft membrane for interaction with downstream effectors. However, the cytosolic domain of NgBR itself is only partially folded. The lack of several conserved secondary structural elements makes this domain unlikely to form a complete farnesyl binding pocket. We find that inclusion of the extracellular and transmembrane domains that contain additional conserved residues to the cytosolic region results in a well folded protein with a similar size and shape to the E.coli cis-isoprenyl transferase (UPPs). Small Angle X-ray Scattering (SAXS) analysis reveals the radius of gyration (Rg) of our NgBR construct to be 18.2 Å with a maximum particle dimension (Dmax) of 61.0 Å. Ab initio shape modeling returns a globular molecular envelope with an estimated molecular weight of 23.0 kD closely correlated with the calculated molecular weight. Both Kratky plot and pair distribution function of NgBR scattering reveal a bell shaped peak which is characteristic of a single globularly folded protein. In addition, circular dichroism (CD) analysis reveals that our construct has the secondary structure contents similar to the UPPs. However, this result does not agree with the currently accepted topological orientation of NgBR which might partition this construct into three separate domains. This discrepancy suggests another possible NgBR topology and lends insight into a potential molecular basis of how NgBR facilitates farnesylated Ras recruitment.
[Mh] Termos MeSH primário: Receptores de Superfície Celular/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Membrana Celular/metabolismo
Dicroísmo Circular
Citosol/metabolismo
Peso Molecular
Estrutura Secundária de Proteína
Receptores de Superfície Celular/metabolismo
Espalhamento a Baixo Ângulo
Homologia de Sequência de Aminoácidos
Solubilidade
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NUS1 protein, human); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191371


  2 / 39711 MEDLINE  
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[PMID]:28470277
[Au] Autor:Tseng TS; Tsai KC; Chen C
[Ad] Endereço:Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan. bmchinp@ibms.sinica.edu.tw.
[Ti] Título:Characterizing the structure-function relationship reveals the mode of action of a novel antimicrobial peptide, P1, from jumper ant Myrmecia pilosula.
[So] Source:Mol Biosyst;13(6):1193-1201, 2017 Jun 01.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Microbial infections of antibiotic-resistant strains cause serious diseases and have a significant impact on public health worldwide, so novel antimicrobial drugs are urgently needed. Insect venoms, a rich source of bioactive components containing antimicrobial peptides (AMPs), are attractive candidates for new therapeutic agents against microbes. Recently, a novel peptide, P1, identified from the venom of the Australian jumper ant Myrmecia pilosula, showed potent antimicrobial activities against both Gram-negative and Gram-positive bacteria, but its structure-function relationship is unknown. Here, we used biochemical and biophysical techniques coupled with computational simulations to explore the mode of action of P1 interaction with dodecylphosphocholine (DPC) micelles as a model membrane system. Our circular dichroism (CD) and NMR studies revealed an amphipathic α-helical structure for P1 upon interaction with DPC micelles. A paramagnetic relaxation enhancement approach revealed that P1 orients its α-helix segment (F6-G14) into DPC micelles. In addition, the α-helix segment could be essential for membrane permeabilization and antimicrobial activity. Moreover, the arginine residues R8, R11, and R15 significantly contribute to helix formation and membrane-binding affinity. The lysine residue K19 of the C-terminus functionally guides P1 to interact with DPC micelles in the early interaction stage. Our study provides insights into the mode of action of P1, which is valuable in modifying and developing potent AMPs as antibiotic drugs.
[Mh] Termos MeSH primário: Anti-Infecciosos/química
Anti-Infecciosos/farmacologia
Biologia Computacional
[Mh] Termos MeSH secundário: Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/farmacologia
Dicroísmo Circular
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Espectroscopia de Ressonância Magnética
Micelas
Testes de Sensibilidade Microbiana
Estrutura Secundária de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antimicrobial Cationic Peptides); 0 (Micelles)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1039/c6mb00810k


  3 / 39711 MEDLINE  
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[PMID]:28466911
[Au] Autor:Scheller JS; Irvine GW; Wong DL; Hartwig A; Stillman MJ
[Ad] Endereço:Department of Chemistry, The University of Western Ontario, London, Ontario, N6A 5B7, Canada. martin.stillman@uwo.ca.
[Ti] Título:Stepwise copper(i) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions.
[So] Source:Metallomics;9(5):447-462, 2017 May 24.
[Is] ISSN:1756-591X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Copper is a ubiquitous trace metal of vital importance in that it serves as a cofactor in many metalloenzymes. Excess copper becomes harmful if not sequestered appropriately in the cell. As a metal ion chaperone, metallothionein (MT) has been proposed as a key player in zinc and copper homeostasis within the cell. The underlying mechanisms by which MT sequesters and transfers copper ions, and subsequently achieves its proposed biological function remain unknown. Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, we report that the Cu(i) to human apo-MT1a binding mechanism is highly pH-dependent. The 20 relative K -values for the binding of 1 to 20 Cu(i) to the 20 cysteines of MT were obtained from computational simulation of the experimental mass spectral results. These data identified the pH-dependent formation of three sequential but completely different Cu-S clusters, as a function of Cu(i) loading. These data provide the first overall sequence for Cu(i) binding in terms of domain specificity and transient binding site structures. Under cooperative binding at pH 7.4, a series of four clusters form: Cu S , followed by Cu S (ß), then a second Cu S (α), and finally Cu S (α) (x = up to 11). Upon further addition of Cu(i), a mixture of species is formed in a non-cooperative mechanism, saturating the 20 cysteines of MT1a. Using benzoquinone, a cysteine modifier, we were able to confirm that Cu S formed solely in the N-terminal ß-domain, as well as confirming the existence of the presumed Cu S cluster in the α-domain. Based on the results of ESI-MS and computational simulation we were able to identify Cu:MT speciation that resulted in specific emission and CD spectral properties.
[Mh] Termos MeSH primário: Cobre/metabolismo
Metalotioneína/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cobre/química
Seres Humanos
Concentração de Íons de Hidrogênio
Metalotioneína/química
Modelos Moleculares
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MT1A protein, human); 0 (Recombinant Proteins); 789U1901C5 (Copper); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1039/c7mt00041c


  4 / 39711 MEDLINE  
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[PMID]:29335413
[Au] Autor:Abberley JP; Killah R; Walker R; Storey JMD; Imrie CT; Salamonczyk M; Zhu C; Gorecka E; Pociecha D
[Ad] Endereço:Department of Chemistry, King's College, University of Aberdeen, Aberdeen, AB24 3UE, UK.
[Ti] Título:Heliconical smectic phases formed by achiral molecules.
[So] Source:Nat Commun;9(1):228, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chiral symmetry breaking in soft matter is a hot topic of current research. Recently, such a phenomenon was found in a fluidic phase showing orientational order of molecules-the nematic phase; although built of achiral molecules, the phase can exhibit structural chirality-average molecular direction follows a short-pitch helix. Here, we report a series of achiral asymmetric dimers with an odd number of atoms in the spacer, which form twisted structures in nematic as well as in lamellar phases. The tight pitch heliconical nematic (N ) phase and heliconical tilted smectic C (SmC ) phase are formed. The formation of a variety of helical structures is accompanied by a gradual freezing of molecular rotation. In the lowest temperature smectic phase, HexI, the twist is expressed through the formation of hierarchical structure: nanoscale helices and mesoscopic helical filaments. The short-pitch helical structure in the smectic phases is confirmed by resonant X-ray measurements.
[Mh] Termos MeSH primário: Cristais Líquidos/química
Conformação Molecular
Nanoestruturas/química
Transição de Fase
[Mh] Termos MeSH secundário: Dicroísmo Circular
Isomerismo
Microscopia de Força Atômica
Modelos Químicos
Modelos Moleculares
Estrutura Molecular
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02626-6


  5 / 39711 MEDLINE  
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[PMID]:29251806
[Au] Autor:Matthews B
[Ad] Endereço:Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
[Ti] Título:Tools for protein science.
[So] Source:Protein Sci;27(1):6-9, 2018 01.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Proteínas/química
[Mh] Termos MeSH secundário: Animais
Dicroísmo Circular
Microscopia Crioeletrônica
Cristalografia por Raios X
Seres Humanos
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
Análise de Sequência de Proteína
[Pt] Tipo de publicação:EDITORIAL; INTRODUCTORY JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3351


  6 / 39711 MEDLINE  
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[PMID]:28595463
[Au] Autor:Li N; Zeng WL; Luo XL; Yang CR; Zhang YJ; Ding Y; Zhao P
[Ad] Endereço:a Key Laboratory for Forest Resources Conservation and Utilization in the Southwest Mountains of China , Ministry of Education, Southwest Forestry University , Kunming , China.
[Ti] Título:A new arbutin derivative from the leaves of Vaccinium dunalianum wight.
[So] Source:Nat Prod Res;32(1):65-70, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A new arbutin derivative, namely dunalianosides J (1), along with six known compounds, arbutin (2), robustaside A (3), 6'-O-caffeoylarbutin (4), dunalianoside D (5), kaempferol 3-O-ß-D-glucopyranoside (6) and kaempferol 3-O-ß-D-sambubioside (7) were isolated from the leaves of Vaccinium dunalianum Wight (Ericaceae). The structure of 1 was elucidated by extensive 1D and 2D NMR, HR-MS and CD spectroscopic analyses. In which, kaempferol 3-O-ß-D-sambubioside (7) was isolated from the genus Vaccinium for the first time.
[Mh] Termos MeSH primário: Arbutina/análogos & derivados
Arbutina/química
Vaccinium/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Quempferóis/química
Espectroscopia de Ressonância Magnética
Estrutura Molecular
Folhas de Planta/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Kaempferols); APM8UQ3Z9O (astragalin); C5INA23HXF (Arbutin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1333993


  7 / 39711 MEDLINE  
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[PMID]:28592143
[Au] Autor:Pang X; Lin X; Tian Y; Liang R; Wang J; Yang B; Zhou X; Kaliyaperumal K; Luo X; Tu Z; Liu Y
[Ad] Endereço:a CAS Key Laboratory of Tropical Marine Bio-resources and Ecology/Guangdong Key Laboratory of Marine Materia Medica/RNAM Center for Marine Microbiology , South China Sea Institute of Oceanology, Chinese Academy of Sciences , Guangzhou , China.
[Ti] Título:Three new polyketides from the marine sponge-derived fungus Trichoderma sp. SCSIO41004.
[So] Source:Nat Prod Res;32(1):105-111, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Three new polyketides named trichbenzoisochromen A (1), 5,7-dihydroxy-3-methyl -2-(2-oxopropyl)naphthalene-1,4-dione (2) and 7-acetyl-1,3,6-trihydroxyanthracene-9,10- dione (3) together with six known compounds (4-9) were isolated from a sponge-derived fungus Trichoderma sp. SCSIO41004. The structures of three new polyketides (1-3) were determined by the extensive spectroscopic analysis, including 1D, 2D NMR and HRESIMS data. The absolute configuration of compound 1 was confirmed by the specific optical rotation value and CD spectra analyses. Compound 4 exhibited significant inhibitory activity against EV71 with the IC value of 25.7 µM.
[Mh] Termos MeSH primário: Antracenos/química
Antivirais/química
Antivirais/farmacologia
Naftalenos/química
Policetídeos/química
Trichoderma/química
[Mh] Termos MeSH secundário: Animais
Antracenos/farmacologia
Organismos Aquáticos/química
Dicroísmo Circular
Enterovirus Humano A/efeitos dos fármacos
Fermentação
Seres Humanos
Vírus da Influenza A Subtipo H3N2/efeitos dos fármacos
Células K562
Células MCF-7
Espectroscopia de Ressonância Magnética/métodos
Estrutura Molecular
Naftalenos/farmacologia
Policetídeos/farmacologia
Poríferos/microbiologia
Espectrometria de Massas por Ionização por Electrospray
Trichoderma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthracenes); 0 (Antiviral Agents); 0 (Naphthalenes); 0 (Polyketides)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1338286


  8 / 39711 MEDLINE  
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[PMID]:28458029
[Au] Autor:Yergoz F; Hastar N; Cimenci CE; Ozkan AD; Tekinay T; Guler MO; Tekinay AB
[Ad] Endereço:Institute of Materials Science and Nanotechnology, National Nanotechnology Research Center (UNAM), Bilkent University, Ankara, 06800, Turkey.
[Ti] Título:Heparin mimetic peptide nanofiber gel promotes regeneration of full thickness burn injury.
[So] Source:Biomaterials;134:117-127, 2017 Jul.
[Is] ISSN:1878-5905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Burn injuries are one of the most common types of trauma worldwide, and their unique physiology requires the development of specialized therapeutic materials for their treatment. Here, we report the use of synthetic, functional and biodegradable peptide nanofiber gels for the improved healing of burn wounds to alleviate the progressive loss of tissue function at the post-burn wound site. These bioactive nanofiber gels form scaffolds that recapitulate the structure and function of the native extracellular matrix through signaling peptide epitopes, which can trigger angiogenesis through their affinity to basic growth factors. In this study, the angiogenesis-promoting properties of the bioactive scaffolds were utilized for the treatment of a thermal burn model. Following the excision of necrotic tissue, bioactive gels and control solutions were applied topically onto the wound area. The wound healing process was evaluated at 7, 14 and 21 days following injury through histological observations, immunostaining and marker RNA/protein analysis. Bioactive peptide nanofiber-treated burn wounds formed well-organized and collagen-rich granulation tissue layers, produced a greater density of newly formed blood vessels, and exhibited increased re-epithelialization and skin appendage development with minimal crust formation, while non-bioactive peptide nanofibers and the commercial wound dressing 3M™ Tegaderm™ did not exhibit significant efficiency over sucrose controls. Overall, the heparin-mimetic peptide nanofiber gels increased the rate of repair of burn injuries and can be used as an effective means of facilitating wound healing.
[Mh] Termos MeSH primário: Queimaduras/terapia
Géis/química
Heparina/química
Nanofibras/química
Peptídeos/química
Tecidos Suporte/química
[Mh] Termos MeSH secundário: Animais
Dicroísmo Circular
Imuno-Histoquímica
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Microscopia Eletrônica de Varredura
Cicatrização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gels); 0 (Peptides); 9005-49-6 (Heparin)
[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:170502
[St] Status:MEDLINE


  9 / 39711 MEDLINE  
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[PMID]:29336444
[Au] Autor:Protopopova AD; Tsvetkov VB; Varizhuk AM; Barinov NA; Podgorsky VV; Klinov DV; Pozmogova GE
[Ad] Endereço:Biophysics Department, Federal Research and Clinical Center of Physical-Chemical Medicine, Moscow, 119435, Russia. klinov.dmitry@mail.ru pozmge@gmail.com.
[Ti] Título:The structural diversity of C-rich DNA aggregates: unusual self-assembly of beetle-like nanostructures.
[So] Source:Phys Chem Chem Phys;20(5):3543-3553, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We studied the ability of oligonucleotides C T (n = 2, 5, 7, 9, 12, 25) to form an intermolecular i-motif using circular dichroism, ultra-violet spectroscopy, nuclear magnetic resonance, high-resolution atomic force microscopy, high-performance liquid chromatography, and molecular dynamics simulations. The arrangement of single-stranded oligonucleotides in multimer i-motifs was very unusual: C-tracts of different oligonucleotides followed each other consecutively in order to fold into a closed intermolecular i-motif core with minimal loops (one cytidine in a loop spanning over a minor groove, three cytidines in a loop over a major groove); intact T-tracts protruded from predefined loci allowing visualization of beetle-like nanostructures by atomic force microscopy. The same structures were formed from analogous biotinylated oligonucleotides demonstrating one of the potential applications of such structures as carriers of multiple functional groups. Our findings open up possibilities for the rational design of pH-sensitive DNA aggregates and evaluation of the efficiency of their assembly.
[Mh] Termos MeSH primário: Nanoestruturas/química
Oligonucleotídeos/química
[Mh] Termos MeSH secundário: Sequência de Bases
Dicroísmo Circular
Microscopia de Força Atômica
Simulação de Dinâmica Molecular
Ressonância Magnética Nuclear Biomolecular
Conformação de Ácido Nucleico
Oligonucleotídeos/síntese química
Espectrofotometria Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligonucleotides)
[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:180117
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp05380k


  10 / 39711 MEDLINE  
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[PMID]:29309999
[Au] Autor:Millan S; Satish L; Bera K; Konar M; Sahoo H
[Ad] Endereço:Department of Chemistry, National Institute of Technology (NIT), Rourkela, Odisha, India.
[Ti] Título:Exploring the effect of 5-Fluorouracil on conformation, stability and activity of lysozyme by combined approach of spectroscopic and theoretical studies.
[So] Source:J Photochem Photobiol B;179:23-31, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:In this present work, a detailed investigation of the effect of an anticancer drug, 5-Fluorouracil (5-FU), on conformation, stability and activity of lysozyme (Lyz) was reported. The interaction between Lyz and 5-FU was reflected in terms of intrinsic fluorescence quenching and change in secondary structure of Lyz. The mode of quenching mechanism involved was evaluated by the steady-state and time-resolved fluorescence measurements. Synchronous and Circular Dichroism (CD) results revealed the conformational changes induced in Lyz upon complexation with 5-FU. Additionally, the effect of temperature and chemical denaturant on the stability of Lyz-5FU complex was carried out. As well as the activity of Lyz in the absence and presence of 5-FU were measured using Micrococcus luteus strain. To support our experimental findings, in vitro interaction between Lyz and 5-FU was done by theoretical studies. The current study will provide a better understanding on the nature of the interactions possible between proteins and drug molecules, which might create a bench mark in medical science in terms of the toxic effect or biological benefits of drug molecules on protein structure and conformation.
[Mh] Termos MeSH primário: Fluoruracila/metabolismo
Modelos Moleculares
Muramidase/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Fluoruracila/química
Guanidina/química
Muramidase/química
Ligação Proteica
Desnaturação Proteica
Estabilidade Proteica
Estrutura Secundária de Proteína
Espectrometria de Fluorescência
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.17 (Muramidase); JU58VJ6Y3B (Guanidine); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE



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