Base de dados : MEDLINE
Pesquisa : D12.644.050 [Categoria DeCS]
Referências encontradas : 9783 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 979 ir para página                         

  1 / 9783 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  2 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28747178
[Au] Autor:Durnas B; Piktel E; Watek M; Wollny T; Gózdz S; Smok-Kalwat J; Niemirowicz K; Savage PB; Bucki R
[Ad] Endereço:Department of Microbiology and Immunology, The Faculty of Health Sciences of the Jan Kochanowski University in Kielce, Kielce, Poland.
[Ti] Título:Anaerobic bacteria growth in the presence of cathelicidin LL-37 and selected ceragenins delivered as magnetic nanoparticles cargo.
[So] Source:BMC Microbiol;17(1):167, 2017 Jul 26.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cationic antibacterial peptides (CAPs) and synthetic molecules mimicking the amphiphilic structure of CAPs, such as ceragenins, are promising compounds for the development of new antimicrobials. RESULTS: We tested the in vitro activity of ceragenins CSA-13 and CSA-131 against several anaerobic bacteria including Bacteroides spp. and Clostridium difficile. We compared results to the activity of cathelicidin LL-37, metronidazole and nanosystems developed by attachment of CSA-13 and CSA-131 to magnetic nanoparticles (MNPs). The antibacterial effect was tested using killing assay and modified CLSI broth microdilution assay. Ceragenins CSA-13 and CSA-131 displayed stronger bactericidal activity than LL-37 or metronidazole against all of the tested bacterial strains. Additionally CSA-131 revealed an enhanced ability to prevent the formation of Bacteroides fragilis and Propionibacterium acnes biofilms. CONCLUSIONS: These data confirmed that ceragenins display antimicrobial activity against a broad range of microorganisms including anaerobic bacteria and deserve further investigations as compounds serving to develop new treatment against anaerobic and mixed infections.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Bactérias Anaeróbias/efeitos dos fármacos
Bactérias Anaeróbias/crescimento & desenvolvimento
Nanopartículas de Magnetita/química
Pregnanos/farmacologia
Esteroides/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/química
Peptídeos Catiônicos Antimicrobianos/química
Pregnanos/química
Esteroides/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (Magnetite Nanoparticles); 0 (Pregnanes); 0 (Steroids); 0 (ceragenin CSA-13); 143108-26-3 (CAP18 lipopolysaccharide-binding protein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-017-1075-6


  3 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28460447
[Au] Autor:Dou X; Han J; Song W; Dong N; Xu X; Zhang W; Shan A
[Ad] Endereço:Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, P.R. China.
[Ti] Título:Sodium butyrate improves porcine host defense peptide expression and relieves the inflammatory response upon Toll-like receptor 2 activation and histone deacetylase inhibition in porcine kidney cells.
[So] Source:Oncotarget;8(16):26532-26551, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Host defense peptides (HDPs) are an important component of the innate immune system and possess direct antimicrobial and immunomodulatory activities. Dietary regulation of HDPs synthesis has emerged as a novel non-antibiotic approach to combat pathogen infection. There are species- and tissue-dependent characteristics of the regulation and mechanism of HDPs. In this study, we investigated whether the histone deacetylase inhibitor (HDACi) sodium butyrate (NaB) could induce HDP expression and the mechanism underlying NaB-regulated HDP expression in PK-15 cells. Our results revealed that NaB augmented HDP expression in PK-15 cells, including porcine ß-defensin 3 (pBD3), epididymis protein 2 splicing variant C (pEP2C), pBD128, pBD123, and pBD115, but no inflammatory response occurred. Inhibition of HDAC activity was not sufficient to induce the expression of pBD3 and pEP2C in comparisons of NaB and another HDACi, trichostatin A (TSA). Concomitantly, NF-κB activation was involved in the induction of HDP expression by NaB. MAPK pathway inhibition also prevented pBD3 and pEP2C induction by NaB. Furthermore, NaB could still promote pBD3 and pEP2C expression and inhibit IL-6 production in the presence of the toll-like receptor 2 (TLR2) ligand peptidoglycan. Moreover, TLR2 could be activated by both NaB and peptidoglycan, and blocking TLR2 expression suppressed HDP induction. Finally, we further showed that increased pBD3 could decrease cytokine interleukin-18 (IL-18) and increase porcine claudin 15 (pCLDN15) contents, suggesting an immunoregulatory function of pBD3. In conclusion, this work paves the way for using HDACi-NaB to induce porcine kidney defense peptides while limiting the deleterious risk of an inflammatory response.
[Mh] Termos MeSH primário: Ácido Butírico/farmacologia
Defensinas/genética
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Regulação da Expressão Gênica/efeitos dos fármacos
Inibidores de Histona Desacetilases/farmacologia
Receptor 2 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Peptídeos Catiônicos Antimicrobianos/genética
Linhagem Celular
Células Cultivadas
Citocinas/genética
Citocinas/metabolismo
Mediadores da Inflamação
Rim
Ligantes
NF-kappa B/metabolismo
Transdução de Sinais/efeitos dos fármacos
Suínos
Receptor 2 Toll-Like/agonistas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Cytokines); 0 (Defensins); 0 (Histone Deacetylase Inhibitors); 0 (Inflammation Mediators); 0 (Ligands); 0 (NF-kappa B); 0 (Toll-Like Receptor 2); 107-92-6 (Butyric Acid)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15714


  4 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29329001
[Au] Autor:Li Z; Wang X; Teng D; Mao R; Hao Y; Yang N; Chen H; Wang X; Wang J
[Ad] Endereço:Key Laboratory of Feed Biotechnology, Ministry of Agriculture, Beijing 100081, People's Republic of China; Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China.
[Ti] Título:Improved antibacterial activity of a marine peptide-N2 against intracellular Salmonella typhimurium by conjugating with cell-penetrating peptides-bLFcin /Tat .
[So] Source:Eur J Med Chem;145:263-272, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Salmonellae, gram-negative bacteria, are facultative intracellular pathogens that cause a number of diseases in animals and humans. The poor penetration ability of antimicrobial agents limits their use in the treatment of intracellular bacterial infections. In this study, the cell-penetrating peptides (CPPs) bLFcin and Tat were separately conjugated to the antimicrobial peptide N2, and the antibacterial activity and pharmacodynamics of the CPPs-N2 conjugates were first evaluated against Salmonellae typhimurium in vitro and in macrophage cells. The cytotoxicity, cellular uptake and mechanism of cellular internalization of the CPPs-N2 conjugates were also examined in RAW264.7 cells. Similar to N2, CPPs-N2 have two reverse ß-sheets and three loops. The minimal inhibitory concentration (MIC) of CPPs-N2 was approximately 2 µM, which was higher than that of N2 (0.8 µM). The dose-time curves and cytotoxicity assay showed that both peptide conjugates were more effective than N2 alone at concentrations ranging from 0.25 to 1 × MIC, and they exhibited low cytotoxicity (9.78%-13.54%) at 100 µM. After 0.5 h incubation, the cell internalization ratio of B6N2 and T11N2 exceeded 28.3% and 93.5%, respectively, which was higher than that of N2. The uptake of B6N2 and T11N2 was reduced by low temperature (82.1%-91.7%), chlorpromazine (35.7%-75.1%), and amiloride (26.0%-52.1%), indicating that macropinocytosis and clathrin-mediated endocytosis may be involved. Approximately 98.85% and 91.35% of bacteria were killed within 3 h by T11N2 and B6N2, respectively, which was higher than the percentage killed by N2 (69.74%). Compared with the bactericidal activity of N2 alone, the bactericidal activity of T11N2 and B6N2 was increased by 53.7%-99.6% and 85.3-85.8%, respectively. Both CPPs-N2 conjugates may be excellent candidates for novel antimicrobial agents to treat infectious diseases caused by intracellular pathogens.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Peptídeos Penetradores de Células/farmacologia
Salmonella typhimurium/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antibacterianos/síntese química
Antibacterianos/química
Peptídeos Catiônicos Antimicrobianos/síntese química
Peptídeos Catiônicos Antimicrobianos/química
Sobrevivência Celular/efeitos dos fármacos
Peptídeos Penetradores de Células/química
Relação Dose-Resposta a Droga
Macrófagos/efeitos dos fármacos
Camundongos
Testes de Sensibilidade Microbiana
Estrutura Molecular
Células RAW 264.7
Salmonella typhimurium/citologia
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (Cell-Penetrating Peptides)
[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:180113
[St] Status:MEDLINE


  5 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28457962
[Au] Autor:Khara JS; Obuobi S; Wang Y; Hamilton MS; Robertson BD; Newton SM; Yang YY; Langford PR; Ee PLR
[Ad] Endereço:Department of Pharmacy, National University of Singapore, 18 Science Drive 4, Singapore 117543, Singapore; Section of Paediatrics, Department of Medicine, St Mary's Campus, Imperial College London, London W2 1PG, United Kingdom; MRC Centre for Molecular Bacteriology and Infection, Department of Medi
[Ti] Título:Disruption of drug-resistant biofilms using de novo designed short α-helical antimicrobial peptides with idealized facial amphiphilicity.
[So] Source:Acta Biomater;57:103-114, 2017 Jul 15.
[Is] ISSN:1878-7568
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The escalating threat of antimicrobial resistance has increased pressure to develop novel therapeutic strategies to tackle drug-resistant infections. Antimicrobial peptides have emerged as a promising class of therapeutics for various systemic and topical clinical applications. In this study, the de novo design of α-helical peptides with idealized facial amphiphilicities, based on an understanding of the pertinent features of protein secondary structures, is presented. Synthetic amphiphiles composed of the backbone sequence (X Y Y X ) , where X and X are hydrophobic residues (Leu or Ile or Trp), Y and Y are cationic residues (Lys), and n is the number repeat units (2 or 2.5 or 3), demonstrated potent broad-spectrum antimicrobial activities against clinical isolates of drug-susceptible and multi-drug resistant bacteria. Live-cell imaging revealed that the most selective peptide, (LKKL) , promoted rapid permeabilization of bacterial membranes. Importantly, (LKKL) not only suppressed biofilm growth, but effectively disrupted mature biofilms after only 2h of treatment. The peptides (LKKL) and (WKKW) suppressed the production of LPS-induced pro-inflammatory mediators to levels of unstimulated controls at low micromolar concentrations. Thus, the rational design strategies proposed herein can be implemented to develop potent, selective and multifunctional α-helical peptides to eradicate drug-resistant biofilm-associated infections. STATEMENT OF SIGNIFICANCE: Antimicrobial peptides (AMPs) are increasingly explored as therapeutics for drug-resistant and biofilm-related infections to help expand the size and quality of the current antibiotic pipeline in the face of mounting antimicrobial resistance. Here, synthetic peptides rationally designed based upon principles governing the folding of natural α-helical AMPs, comprising the backbone sequence (X Y Y X ) , and which assemble into α-helical structures with idealized facial amphiphilicity, is presented. These multifunctional peptide amphiphiles demonstrate high bacterial selectivity, promote the disruption of pre-formed drug-resistant biofilms, and effectively neutralize endotoxins at low micromolar concentrations. Overall, the design strategies presented here could provide a useful tool for developing therapeutic peptides with broad-ranging clinical applications from the treatment and prevention of drug-resistant biofilms to the neutralization of bacterial endotoxins.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/química
Bactérias/crescimento & desenvolvimento
Biofilmes
Farmacorresistência Bacteriana
Endotoxinas/química
[Mh] Termos MeSH secundário: Fenômenos Fisiológicos Bacterianos
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Endotoxins)
[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:170502
[St] Status:MEDLINE


  6 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29366788
[Au] Autor:Yoshida K; Murayama MA; Shimizu K; Tang C; Katagiri N; Matsuo K; Fukai F; Iwakura Y
[Ad] Endereço:Center for Animal Disease Models, Research Institute for Biomedical Sciences (RIBS), Tokyo University of Science (TUS), Chiba, 278-0022, Japan; Department of Pharmaceutical Sciences, Graduate School of Pharmaceutical Sciences, TUS, Chiba, 278-0022, Japan.
[Ti] Título:IL-1R2 deficiency suppresses dextran sodium sulfate-induced colitis in mice via regulation of microbiota.
[So] Source:Biochem Biophys Res Commun;496(3):934-940, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ulcerative colitis (UC) is an inflammatory disease of the colon. IL1R2, which encodes IL-1 receptor type 2 (IL-1R2), was reported as a risk gene for UC. To elucidate the roles of IL-1R2 in the development of colitis, we examined the development of dextran sodium sulfate-induced colitis, a mouse model for UC using Il1r2 mice. We found the severity score of colitis was milder in Il1r2 mice compared with wild-type (WT) mice when they were housed separately, however the severity score was similar when they were housed in a cage. In the separate housing condition, relative contents of Actinobacteria and Bacilli in feces of Il1r2 mice were lower than that of WT mice. Furthermore, IL-1ß induced the expression of antimicrobial peptides (AMPs) from colon. Thus, we show that IL-1R2 is harmful for the development of colitis, because IL-1R2 promotes the growth of proinflammatory intestinal microbiota by suppressing IL-1ß-induced AMP production.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/imunologia
Colite/imunologia
Microbioma Gastrointestinal/imunologia
Receptores de Interleucina-1/imunologia
[Mh] Termos MeSH secundário: Animais
Colite/induzido quimicamente
Colite/patologia
Sulfato de Dextrana
Feminino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Receptores de Interleucina-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Receptors, Interleukin-1); 0 (interleukin-36 receptor, mouse); 9042-14-2 (Dextran Sulfate)
[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


  7 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29191658
[Au] Autor:Sang M; Wu Q; Xi X; Ma C; Wang L; Zhou M; Burrows JF; Chen T
[Ad] Endereço:School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, Jiangsu, 210023, China; School of Pharmacy, Queen's University, Belfast BT9 7BL, Northern Ireland, UK.
[Ti] Título:Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus.
[So] Source:Biochem Biophys Res Commun;495(4):2539-2546, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A potent natural antimicrobial peptide named temporin-PE was identified and encoded from the skin secretions of Pelophylax kl. esculentus via "shotgun" cloning and LC-MS/MS fragmentation analysis. Target-modifications were carried out to further enhance the antimicrobial and anti-proliferative bioactivities, whilst decreasing the hemolytic effect. A range of bioassays demonstrated that replacing a proline with a tyrosine residue resulted in a loss of the bioactivity against Gram-negative bacteria, but dramatically improved the hemolytic and anti-proliferative activity, indicating the FLP- motif influences the hemolytic activity of temporins. Moreover, the coupling of TAT to the peptide dramatically improved its antimicrobial activity, indicating coupling TAT to these peptides could be considered as a potential tool to improve their antimicrobial activity. Overall, we have shown that targeted modifications of this natural antimicrobial peptide can adjust its bioactivities to help its development as an antibiotic or anti-proliferative agent.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/química
Peptídeos Catiônicos Antimicrobianos/administração & dosagem
Peptídeos Catiônicos Antimicrobianos/química
Fenômenos Fisiológicos Bacterianos/efeitos dos fármacos
Rana esculenta/metabolismo
Pele/secreção
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/administração & dosagem
Proteínas de Anfíbios/secreção
Animais
Antibacterianos/administração & dosagem
Antibacterianos/química
Antibacterianos/isolamento & purificação
Peptídeos Catiônicos Antimicrobianos/secreção
Sobrevivência Celular/efeitos dos fármacos
Dados de Sequência Molecular
Pele/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (temporin-PE, Pelophylax kl. esculentus)
[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:171202
[St] Status:MEDLINE


  8 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28461043
[Au] Autor:Pei J; Jiang L
[Ad] Endereço:Shaanxi Key Laboratory of Biology and Bioresources, Shaanxi University of Technology, Chaoyang Road, Hanzhong, Shaanxi 723001, China. Electronic address: jinjinpeislg@163.com.
[Ti] Título:Antimicrobial peptide from mucus of Andrias davidianus: screening and purification by magnetic cell membrane separation technique.
[So] Source:Int J Antimicrob Agents;50(1):41-46, 2017 Jul.
[Is] ISSN:1872-7913
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Andrias davidianus, the Chinese giant salamander, has been used in traditional Chinese medicine for many decades. However, no antimicrobial peptides (AMPs) have been described from A. davidianus until now. Here we describe a novel AMP (andricin 01) isolated from the mucus of A. davidianus. The peptide was recovered using an innovative magnetic cell membrane separation technique and was characterised using mass spectrometry and circular dichroism (CD) spectroscopy. Andricin 01 is comprised of ten amino acid residues with a total molecular mass of 955.1 Da. CD spectrum analysis gave results similar to the archetypal random coil spectrum, consistent with the three-dimensional rendering calculated by current bioinformatics tools. Andricin 01 was found to be inhibitory both to Gram-negative and Gram-positive bacteria. Furthermore, the peptide at the minimal bacterial concentration did not show cell cytotoxicity against human hepatocytes or renal cells and did not show haemolytic activity against red blood cells, indicating that is potentially safe and effective for human use. Andricin 01 shows promise as a novel antibacterial that may provide an insight into the development of new drugs.
[Mh] Termos MeSH primário: Anti-Infecciosos/isolamento & purificação
Anti-Infecciosos/farmacologia
Peptídeos Catiônicos Antimicrobianos/isolamento & purificação
Peptídeos Catiônicos Antimicrobianos/farmacologia
Bactérias/efeitos dos fármacos
Muco/química
Urodelos
[Mh] Termos MeSH secundário: Animais
Anti-Infecciosos/química
Anti-Infecciosos/toxicidade
Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/toxicidade
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Dicroísmo Circular
Hepatócitos/efeitos dos fármacos
Seres Humanos
Programas de Rastreamento/métodos
Espectrometria de Massas
Peso Molecular
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antimicrobial Cationic Peptides)
[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:170503
[St] Status:MEDLINE


  9 / 9783 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29193264
[Au] Autor:Kausar S; Abbas MN; Qian C; Zhu B; Gao J; Sun Y; Wang L; Wei G; Liu C
[Ad] Endereço:College of Life Sciences, Anhui Agricultural University, Hefei, China.
[Ti] Título:Role of Antheraea pernyi serpin 12 in prophenoloxidase activation and immune responses.
[So] Source:Arch Insect Biochem Physiol;97(2), 2018 Feb.
[Is] ISSN:1520-6327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serine protease inhibitors play a key role in the immune system of invertebrates by controlling proteolytic cascades. Besides its importance, the knowledge on immune functions of serpins in most of insects is fragmentary. In the present study, we identified serpin-12 from Antheraea pernyi encoding a predicted 402 amino acid residue protein (Apserpin-12). We expressed the recombinant protein in Escherichia coli and the purified protein was used for the synthesis of rabbit anti-Apserpin-12 polyclonal antibodies and functional studies. Quantitative real-time ploymerase chain reaction (qRT-PCR) analysis revealed that the knock-down of Apserpin-12 enhanced the prophenoloxidase (PPO) cascade stimulated by Micrococcus luteus in hemolymph, whereas addition of recombinant Apserpin-12 protein along with same elicitor led to down-regulate PPO activation. Following different microbial challenge (E. coli, Beauveria bassiana, M. Luteus, and nuclear polyhedrosis virus), the expression of Apserpin-12 mRNA was induced significantly. Furthermore, the Apserpin-12 double-stranded RNA administration elicited the expression of antimicrobial peptides, while the treatment with recombinant protein suppressed their expression. Tissue profile of Apserpin-12 indicated that it is expressed in all examined tissues, that is, hemolymph, malpighian tubules, midgut, silk gland, integument, and fat body with variation in their transcript levels. We concluded that Apserpin-12 may regulate PPO activation and inhibit the production of antimicrobial peptides in A. pernyi, suggesting important role in its immune system.
[Mh] Termos MeSH primário: Catecol Oxidase/metabolismo
Precursores Enzimáticos/metabolismo
Mariposas/química
Serpinas/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Peptídeos Catiônicos Antimicrobianos/metabolismo
Ativação Enzimática
Escherichia coli
Mariposas/fisiologia
Filogenia
Serpinas/química
Serpinas/genética
Serpinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Enzyme Precursors); 0 (Serpins); EC 1.10.3.- (pro-phenoloxidase); EC 1.10.3.1 (Catechol Oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1002/arch.21435


  10 / 9783 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
[PMID]:29372793
[Au] Autor:Istomina EA; Korostyleva TV; Rozhnova NA; Rogozhin EA; Pukhalskiy VA; Odintsova TI
[Ti] Título:[Genes encoding hevein-like antimicrobial peptides WAMPs: Expression in response to phytohormones and environmental factors].
[So] Source:Genetika;52(11):1300-10, 2016 Nov.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:We investigated the role of genes of hevein-like antimicrobial peptides of the WAMP family in the protection of wheat plants against biotic and abiotic stress. The semiquantitative RT-PCR method was used to examine the expression of wamp genes in wheat seedlings in response to infection by pathogens and exposure to phytohormones and ions of a heavy metal ion­cadmium. We discovered that wheat germ contamination by harmful fungi significantly increases expression of genes of the wamp family, and the primary transcript is wamp-2. We determined that salicylic acid, rather than methyl jasmonate, induces expression of genes of the wamp family. We showed that abiotic stress induced by cadmium ions inhibits expression of wamp genes in the roots with no effect on their expression in shoots. The results support the protective role of wamp genes in the response of wheat plants to infections by pathogens. In turn, the resistance to abiotic stress induced by cadmium ions does not appear to be associated with expression of genes of the wamp family.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/biossíntese
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Genes de Plantas/fisiologia
Reguladores de Crescimento de Planta/farmacologia
Lectinas de Plantas/biossíntese
Caules de Planta/metabolismo
Triticum/metabolismo
[Mh] Termos MeSH secundário: Peptídeos Catiônicos Antimicrobianos/genética
Regulação da Expressão Gênica de Plantas/fisiologia
Lectinas de Plantas/genética
Caules de Planta/genética
Triticum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Plant Growth Regulators); 0 (Plant Lectins); 137295-60-4 (hevein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE



página 1 de 979 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde