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[PMID]:29432422
[Au] Autor:Mathur D; Mehta A; Firmal P; Bedi G; Sood C; Gautam A; Raghava GPS
[Ad] Endereço:Bioinformatics Centre, CSIR-Institute of Microbial Technology, Chandigarh, India.
[Ti] Título:TopicalPdb: A database of topically delivered peptides.
[So] Source:PLoS One;13(2):e0190134, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:TopicalPdb (http://crdd.osdd.net/raghava/topicalpdb/) is a repository of experimentally verified topically delivered peptides. Data was manually collected from research articles. The current release of TopicalPdb consists of 657 entries, which includes peptides delivered through the skin (462 entries), eye (173 entries), and nose (22 entries). Each entry provides comprehensive information related to these peptides like the source of origin, nature of peptide, length, N- and C-terminal modifications, mechanism of penetration, type of assays, cargo and biological properties of peptides, etc. In addition to natural peptides, TopicalPdb contains information of peptides having non-natural, chemically modified residues and D-amino acids. Besides this primary information, TopicalPdb stores predicted tertiary structures as well as peptide sequences in SMILE format. Tertiary structures of peptides were predicted using state-of-art method PEPstrMod. In order to assist users, a number of web-based tools have been integrated that includes keyword search, data browsing, similarity search and structural similarity. We believe that TopicalPdb is a unique database of its kind and it will be very useful in designing peptides for non-invasive topical delivery.
[Mh] Termos MeSH primário: Bases de Dados de Proteínas
Peptídeos/química
[Mh] Termos MeSH secundário: Administração Tópica
Peptídeos/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides)
[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:180213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190134


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[PMID]:29309431
[Au] Autor:Carmalt JL; Mortazavi S; McOnie RC; Allen AL; Unniappan S
[Ad] Endereço:Department of Large Animal Clinical Sciences, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon, SK, Canada.
[Ti] Título:Profiles of pro-opiomelanocortin and encoded peptides, and their processing enzymes in equine pituitary pars intermedia dysfunction.
[So] Source:PLoS One;13(1):e0190796, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Equine pituitary pars intermedia dysfunction (PPID) is characterized by hyperplasia of the pars intermedia (PI) melanotrophs of the pituitary gland (PG), and increased production of proopiomelanocortin (POMC). POMC is cleaved by prohormone convertase 1 (PC1) to produce adrenocorticotropic hormone (ACTH), and further processing of ACTH by PC2 to produce alpha-melanocyte stimulating hormone (α-MSH) and corticotropin-like intermediate peptide (CLIP). High plasma ACTH concentrations in horses with PPID might be related to reduced conversion of ACTH to α-MSH by PCs. The hypothesis of this study was that PC1 and PC2 expression in the pituitary gland are altered in PPID, resulting in an abnormal relative abundance of POMC derived proteins. The objectives of this study were to identify the partial sequences of equine POMC, PC1, and PC2 mRNAs; and to determine whether the expression of POMC, PC1, and PC2 mRNAs in whole pituitary extracts, and POMC-protein in the cavernous sinus blood of horses are altered in PPID. We confirmed (RT-PCR and sequencing) that the partial sequences obtained match the corresponding regions of predicted equine POMC, PC1 and PC2 sequences. The expression (quantification by RT-qPCR) of POMC, PC1 and PC2 mRNAs were found upregulated in the pituitary of horses with PPID. Plasma (measured using RIA/ELISA) ACTH and α-MSH were elevated in PPID horses. These results indicate distinct differences in gene and protein expression of POMC and its intermediates, and processing enzymes in PPID. It provides evidence to support the notion that local, pituitary-specific inadequacies in prohormone processing likely contribute to equine PPID.
[Mh] Termos MeSH primário: Peptídeos/metabolismo
Adeno-Hipófise Parte Intermédia/metabolismo
Pró-Opiomelanocortina/metabolismo
[Mh] Termos MeSH secundário: Hormônio Adrenocorticotrópico/sangue
Sequência de Aminoácidos
Animais
Ensaio de Imunoadsorção Enzimática
Cavalos
Adeno-Hipófise Parte Intermédia/enzimologia
Pró-Opiomelanocortina/sangue
Pró-Opiomelanocortina/química
Pró-Opiomelanocortina/genética
Pró-Proteína Convertase 1/genética
Pró-Proteína Convertase 1/metabolismo
Pró-Proteína Convertase 2/genética
Pró-Proteína Convertase 2/metabolismo
RNA Mensageiro/metabolismo
Homologia de Sequência de Aminoácidos
alfa-MSH/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0 (RNA, Messenger); 581-05-5 (alpha-MSH); 66796-54-1 (Pro-Opiomelanocortin); 9002-60-2 (Adrenocorticotropic Hormone); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2)
[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:180109
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190796


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[PMID]:29272750
[Au] Autor:Galibert M; Wartenberg M; Lecaille F; Saidi A; Mavel S; Joulin-Giet A; Korkmaz B; Brömme D; Aucagne V; Delmas AF; Lalmanach G
[Ad] Endereço:CNRS UPR 4301, Centre de Biophysique Moléculaire, Rue Charles Sadron, Orléans, France.
[Ti] Título:Substrate-derived triazolo- and azapeptides as inhibitors of cathepsins K and S.
[So] Source:Eur J Med Chem;144:201-210, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Cathepsin (Cat) K is a critical bone-resorbing protease and is a relevant target for the treatment of osteoporosis and bone metastasis, while CatS is an attractive target for drugs in autoimmune diseases (e.g. rheumatoid arthritis), emphysema or neuropathic pain. Despite major achievements, current pharmacological inhibitors are still lacking in safety and may have damaging side effects. A promising strategy for developing safer reversible and competitive inhibitors as new lead compounds could be to insert non-cleavable bonds at the scissile P1-P1' position of selective substrates of CatS and CatK. Accordingly, we introduced a 1,4-disubstituted 1,2,3-triazole heterocycle that mimics most of the features of a trans-amide bond, or we incorporated a semicarbazide bond (azaGly residue) by replacing the α-carbon of the glycyl residue at P1 by a nitrogen atom. AzaGly-containing peptidomimetics inhibited powerfully their respective target proteases in the nM range, while triazolopeptides were weaker inhibitors (Ki in the µM range). The selectivity of the azaGly CatS inhibitor (1b) was confirmed by using spleen lysates from wild-type vs CatS-deficient mice. Alternatively, the azaGly bradykinin-derived CatK inhibitor (2b) potently inhibited CatK (Ki = 9 nM) and impaired its kininase activity in vitro. Molecular modeling studies support that the semicarbazide bond of 2b is more favorable than the 1,2,3-triazole linkage of the bradykinin-derived pseudopeptide 2a to preserve an effective affinity towards CatK, its protease target.
[Mh] Termos MeSH primário: Catepsina K/antagonistas & inibidores
Catepsinas/antagonistas & inibidores
Inibidores de Proteases/química
Inibidores de Proteases/farmacologia
Triazóis/química
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Catepsina K/metabolismo
Catepsinas/metabolismo
Seres Humanos
Camundongos Endogâmicos C57BL
Simulação de Acoplamento Molecular
Peptídeos/química
Peptídeos/farmacologia
Peptidomiméticos/química
Peptidomiméticos/farmacologia
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Peptidomimetics); 0 (Protease Inhibitors); 0 (Triazoles); EC 3.4.- (Cathepsins); EC 3.4.22.27 (cathepsin S); EC 3.4.22.38 (Cathepsin K)
[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:171223
[St] Status:MEDLINE


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[PMID]:29200855
[Au] Autor:Gerstenhaber JA; Barone FC; Marcinkiewicz C; Li J; Shiloh AO; Sternberg M; Lelkes PI; Feuerstein G
[Ad] Endereço:Department of Bioengineering, College of Engineering, Temple University, Philadelphia, PA.
[Ti] Título:Vascular thrombus imaging in vivo via near-infrared fluorescent nanodiamond particles bioengineered with the disintegrin bitistatin (Part II).
[So] Source:Int J Nanomedicine;12:8471-8482, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:The aim of this feasibility study was to test the ability of fluorescent nanodiamond particles (F-NDP) covalently conjugated with bitistatin (F-NDP-Bit) to detect vascular blood clots in vivo using extracorporeal near-infrared (NIR) imaging. Specifically, we compared NIR fluorescence properties of F-NDP with N-V (F-NDP ) and N-V-N color centers and sizes (100-10,000 nm). Optimal NIR fluorescence and tissue penetration across biological tissues (rat skin, porcine axillary veins, and skin) was obtained for F-NDP with a mean diameter of 700 nm. Intravital imaging (using in vivo imaging system [IVIS]) in vitro revealed that F-NDP -loaded glass capillaries could be detected across 6 mm of rat red-muscle barrier and 12 mm of porcine skin, which equals the average vertical distance of a human carotid artery bifurcation from the surface of the adjacent skin (14 mm). In vivo, feasibility was demonstrated in a rat model of occlusive blood clots generated using FeCl in the carotid artery bifurcation. Following systemic infusions of F-NDP -Bit (3 or 15 mg/kg) via the external carotid artery or femoral vein (N=3), presence of the particles in the thrombi was confirmed both in situ via IVIS, and ex vivo via confocal imaging. The presence of F-NDP in the vascular clots was further confirmed by direct counting of fluorescent particles extracted from clots following tissue solubilization. Our data suggest that F-NDP -Bit associate with vascular blood clots, presumably by binding of F-NDP -Bit to activated platelets within the blood clot. We posit that F-NDP -Bit could serve as a noninvasive platform for identification of vascular thrombi using NIR energy monitored by an extracorporeal device.
[Mh] Termos MeSH primário: Bioengenharia/métodos
Diagnóstico por Imagem
Desintegrinas/química
Raios Infravermelhos
Nanodiamantes/química
Peptídeos/química
Trombose/diagnóstico
[Mh] Termos MeSH secundário: Animais
Artérias Carótidas/patologia
Modelos Animais de Doenças
Desintegrinas/administração & dosagem
Fluorescência
Seres Humanos
Infusões Intravenosas
Masculino
Peptídeos/administração & dosagem
Ratos Sprague-Dawley
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disintegrins); 0 (Nanodiamonds); 0 (Peptides); 124123-27-9 (bitistatin)
[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:171205
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S146946


  5 / 140926 MEDLINE  
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[PMID]:29024724
[Au] Autor:Urban C; Buck A; Siveke JT; Lordick F; Luber B; Walch A; Aichler M
[Ad] Endereço:Research Unit Analytical Pathology, Helmholtz Zentrum München, Neuherberg, Germany. Electronic address: christian.urban@helmholtz-muenchen.de.
[Ti] Título:PAXgene fixation enables comprehensive metabolomic and proteomic analyses of tissue specimens by MALDI MSI.
[So] Source:Biochim Biophys Acta;1862(1):51-60, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An alcohol-based non-crosslinking tissue fixative, PAXgene Tissue System, has been proposed as alternative fixation method to formalin, providing superior and morphological preservation. To date, metabolites have not been assessed in PAXgene-fixed tissues. The study focuses on a comparison between PAXgene and standard formalin fixation for metabolomic analysis by MALDI mass spectrometry imaging. Therefore, fifty-six samples from seven mice organs were fixed with PAXgene (PFPE) or formalin (FFPE), embedded in paraffin, and processed to a tissue microarray. PAXgene was able to spatially preserve metabolites in organs achieving an overlap of common metabolites ranging from 34 to 78% with FFPE. Highly similar signal intensities and visualization of molecules demonstrated negligible differences for metabolite imaging on PFPE compared to FFPE tissues. In addition, we performed proteomic analysis of intact proteins and peptides derived from enzymatic digestion. An overlap of 33 to 58% was found between FFPE and PFPE tissue samples in peptide analysis with a higher number of PFPE-specific peaks. Analysis of intact proteins achieved an overlap in the range of 0 to 28% owing to the poor detectability of cross-linked proteins in formalin-fixed tissues. Furthermore, metabolite and peptide profiles obtained from PFPE tissues were able to correctly classify organs independent of the fixation method, whereas a distinction of organs by protein profiles was only achieved by PAXgene fixation. Finally, we applied MALDI MSI to human biopsies by sequentially analyzing metabolites and peptides within the same tissue section. Concerning prospective studies, PAXgene can be used as an alternative fixative for multi-omic tissue analysis.
[Mh] Termos MeSH primário: Fixadores/química
Metabolômica/métodos
Proteômica/métodos
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
Fixação de Tecidos/métodos
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Camundongos
Peptídeos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fixatives); 0 (Peptides)
[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:171013
[St] Status:MEDLINE


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[PMID]:28844981
[Au] Autor:Gogineni V; Hamann MT
[Ad] Endereço:Department of BioMolecular Sciences, Division of Medicinal Chemistry, School of Pharmacy, The University of Mississippi, University, MS, United States. Electronic address: vgoginen@go.olemiss.edu.
[Ti] Título:Marine natural product peptides with therapeutic potential: Chemistry, biosynthesis, and pharmacology.
[So] Source:Biochim Biophys Acta;1862(1):81-196, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The oceans are a uniquely rich source of bioactive metabolites, of which sponges have been shown to be among the most prolific producers of diverse bioactive secondary metabolites with valuable therapeutic potential. Much attention has been focused on marine bioactive peptides due to their novel chemistry and diverse biological properties. As summarized in this review, marine peptides are known to exhibit various biological activities such as antiviral, anti-proliferative, antioxidant, anti-coagulant, anti-hypertensive, anti-cancer, antidiabetic, antiobesity, and calcium-binding activities. This review focuses on the chemistry and biology of peptides isolated from sponges, bacteria, cyanobacteria, fungi, ascidians, and other marine sources. The role of marine invertebrate microbiomes in natural products biosynthesis is discussed in this review along with the biosynthesis of modified peptides from different marine sources. The status of peptides in various phases of clinical trials is presented, as well as the development of modified peptides including optimization of PK and bioavailability.
[Mh] Termos MeSH primário: Anti-Hipertensivos
Antineoplásicos
Antivirais
Organismos Aquáticos/química
Hipoglicemiantes
Biossíntese Peptídica
Peptídeos
[Mh] Termos MeSH secundário: Animais
Anti-Hipertensivos/química
Anti-Hipertensivos/uso terapêutico
Antineoplásicos/química
Antineoplásicos/uso terapêutico
Antivirais/química
Antivirais/uso terapêutico
Organismos Aquáticos/metabolismo
Seres Humanos
Hipoglicemiantes/química
Hipoglicemiantes/uso terapêutico
Peptídeos/química
Peptídeos/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Antihypertensive Agents); 0 (Antineoplastic Agents); 0 (Antiviral Agents); 0 (Hypoglycemic Agents); 0 (Peptides)
[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:170829
[St] Status:MEDLINE


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[PMID]:28452485
[Au] Autor:Li H; Park J; Kim H; Hwang KB; Paek E
[Ad] Endereço:School of Computer Science and Engineering, Soongsil University , Seoul 06978, Republic of Korea.
[Ti] Título:Systematic Comparison of False-Discovery-Rate-Controlling Strategies for Proteogenomic Search Using Spike-in Experiments.
[So] Source:J Proteome Res;16(6):2231-2239, 2017 Jun 02.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteogenomic searches are useful for novel peptide identification from tandem mass spectra. Usually, separate and multistage approaches are adopted to accurately control the false discovery rate (FDR) for proteogenomic search. Their performance on novel peptide identification has not been thoroughly evaluated, however, mainly due to the difficulty in confirming the existence of identified novel peptides. We simulated a proteogenomic search using a controlled, spike-in proteomic data set. After confirming that the results of the simulated proteogenomic search were similar to those of a real proteogenomic search using a human cell line data set, we evaluated the performance of six FDR control methods-global, separate, and multistage FDR estimation, respectively, coupled to a target-decoy search and a mixture model-based method-on novel peptide identification. The multistage approach showed the highest accuracy for FDR estimation. However, global and separate FDR estimation with the mixture model-based method showed higher sensitivities than others at the same true FDR. Furthermore, the mixture model-based method performed equally well when applied without or with a reduced set of decoy sequences. Considering different prior probabilities for novel and known protein identification, we recommend using mixture model-based methods with separate FDR estimation for sensitive and reliable identification of novel peptides from proteogenomic searches.
[Mh] Termos MeSH primário: Peptídeos/análise
Proteogenômica/métodos
[Mh] Termos MeSH secundário: Linhagem Celular
Simulação por Computador
Reações Falso-Positivas
Seres Humanos
Métodos
Modelos Teóricos
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides)
[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:170429
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.7b00033


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[PMID]:29282749
[Au] Autor:Hou L; Wang J; Wang Y; Hua X; Wu J
[Ad] Endereço:Renji Hospital, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), School of Medicine, Bio-X Institutes, Shanghai Jiao Tong University, Shanghai, China.
[Ti] Título:Compared proteomic analysis of 8- and 32-week-old postnatal porcine ovaries.
[So] Source:Cell Biochem Funct;36(1):34-42, 2018 Jan.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pigs share many anatomical and physiological features with humans, offering a unique and viable model for biomedical research. Tandem mass tag method followed by mass spectrometry analysis was utilized to identify peptides (47,405), proteins (14,701), and protein groups (7634) in ovaries of 8- and 32-week-old postnatal Banna miniature pigs. After annotation and analysis by Kyoto Encyclopedia of Genes and Genomes pathway and Gene Ontology, the proteins were identified as being involved in hormone metabolic pathways and maintenance, proliferation, and regulation of stem cells. In addition, we found 638 differentially expressed proteins between ovaries of 8- and 32-week-old postnatal Banna miniature pigs. We used Interactive Pathway Explorer to produce an overview of pig ovarian proteomics. Compared with those of the 8-week-old group, the proteins enriched in metabolism of steroid hormones, metabolism of lipids, and energy metabolism pathway were upregulated in the 32-week-old group, indicating physiological characteristics of sexual maturity. These findings have implications in applications of biomedicine. SIGNIFICANCE OF THE STUDY: Pigs share many anatomical and physiological features with humans, offering a unique and viable model for biomedical research. In this study, we used tandem mass tag quantitative proteomics to describe, for the first time, protein expression patterns of postnatal pig ovaries. Proteins involved in hormone metabolic pathways and maintenance, proliferation, and regulation of stem cells were identified. With further analysis by Interactive Pathway Explorer, proteins enriched in metabolism of steroid hormones, metabolism of lipids, and energy metabolism pathway were upregulated in the 32-week-old group, indicating physiological characteristics of sexual maturity. These findings have implications in applications of biomedicine.
[Mh] Termos MeSH primário: Ovário/química
Peptídeos/análise
Proteínas/análise
Proteômica
[Mh] Termos MeSH secundário: Animais
Proliferação Celular
Cromatografia Líquida
Feminino
Espectrometria de Massas
Camundongos
Camundongos Nus
Ovário/metabolismo
Peptídeos/metabolismo
Proteínas/metabolismo
Células-Tronco/citologia
Células-Tronco/metabolismo
Suínos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Proteins)
[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:171229
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3315


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[PMID]:28457894
[Au] Autor:Zupancic O; Bernkop-Schnürch A
[Ad] Endereço:Department of Pharmaceutical Technology, Institute of Pharmacy, Leopold-Franzens-University Innsbruck, Innrain 80/82, Center for Chemistry and Biomedicine, 6020 Innsbruck, Austria.
[Ti] Título:Lipophilic peptide character - What oral barriers fear the most.
[So] Source:J Control Release;255:242-257, 2017 Jun 10.
[Is] ISSN:1873-4995
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Peptide therapeutics is currently one of the fastest growing markets worldwide and consequently convenient ways of administration for these drugs are highly on demand. In particular, oral dosage forms would be preferred. A relative large molecular weight and high hydrophilicity, however, result in comparatively very low oral bioavailability being in most cases below 1%. Lipid based formulations (LBF), in particular self-emulsifying drug delivery systems (SEDDS) and solid lipid nanoparticles (SLN) as well as liposomes are among the most promising tools for oral peptide delivery. Key to success in orally delivering peptides via LBF seems to be a sufficiently high lipophilic character of those therapeutic agents. Hence, different non-covalent and covalent peptide lipidization methods from drug delivery point of view are presented. On the one hand, among non-covalent lipidization methods hydrophobic ion pairing seems to be a promising way to sufficiently increase peptide lipophilicity providing high drug payloads in the lipid phase, a protective effect against presystemic metabolism via thiol-disulphide exchange reactions and proteolysis as well as an improved intestinal membrane permeability. On the other hand, covalent methods like conjugating fatty acids via amidation, esterification, reversible aqueous lipidization (REAL) and cyclization also show potential. The present review therefore describes those lipidization methods in detail and critically evaluates their contribution in successfully overcoming the oral barriers.
[Mh] Termos MeSH primário: Lipídeos/química
Peptídeos/química
[Mh] Termos MeSH secundário: Administração Oral
Animais
Sistemas de Liberação de Medicamentos
Seres Humanos
Absorção Intestinal
Peptídeos/administração & dosagem
Peptídeos/farmacocinética
Peptídeos/uso terapêutico
Proteólise
Vacinas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Lipids); 0 (Peptides); 0 (Vaccines)
[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:170502
[St] Status:MEDLINE


  10 / 140926 MEDLINE  
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[PMID]:29311507
[Au] Autor:Sumiyoshi T
[Ad] Endereço:Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University.
[Ti] Título:Foreword.
[So] Source:Chem Pharm Bull (Tokyo);66(1):20, 2018.
[Is] ISSN:1347-5223
[Cp] País de publicação:Japan
[La] Idioma:eng
[Mh] Termos MeSH primário: Peptídeos/farmacologia
Receptores Muscarínicos/metabolismo
[Mh] Termos MeSH secundário: Química Farmacêutica
Descoberta de Drogas
Seres Humanos
Peptídeos/química
[Pt] Tipo de publicação:INTRODUCTORY JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Receptors, Muscarinic)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1248/cpb.c18-ctf6601



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