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  1 / 12942 MEDLINE  
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[PMID]:29184921
[Au] Autor:Jaworek MW; Schuabb V; Winter R
[Ad] Endereço:Physical Chemistry I - Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Otto-Hahn-Strasse 4a, 44227 Dortmund, Germany. roland.winter@tu-dortmund.de.
[Ti] Título:The effects of glycine, TMAO and osmolyte mixtures on the pressure dependent enzymatic activity of α-chymotrypsin.
[So] Source:Phys Chem Chem Phys;20(3):1347-1354, 2018 Jan 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:High pressure is an important feature of certain natural environments, such as the deep sea where pressures up to about 1000 bar are encountered. Further, pressure effects on biosystems are of increasing interest for biotechnological applications, such as baroenzymology. We studied the effect of two different natural osmolyte mixtures, with major components being glycine and trimethylamine-N-oxide (TMAO), on the activity of α-chymotrypsin, using high-pressure stopped-flow methodology in combination with fast UV/Vis detection. We show that pressure is not only able to drastically enhance the catalytic activity and efficiency of the enzyme, but also that glycine has a significant and diverse effect on the enzymatic activity and volumetric properties of the reaction compared to TMAO. The results might not only help to understand the modulation of enzymatic reactions by natural osmolytes, but also elucidate ways to optimize enzymatic processes in biotechnological applications.
[Mh] Termos MeSH primário: Quimotripsina/metabolismo
Glicina/química
Metilaminas/química
[Mh] Termos MeSH secundário: Quimotripsina/química
Glicina/metabolismo
Hidrólise
Cinética
Metilaminas/metabolismo
Concentração Osmolar
Pressão
Especificidade por Substrato
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Methylamines); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.1 (alpha-chymotrypsin); FLD0K1SJ1A (trimethyloxamine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06042d


  2 / 12942 MEDLINE  
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[PMID]:29079225
[Au] Autor:Ibarra-García LE; Tovar-Ramírez D; Rosas C; Campa-Córdova ÁI; Mazón-Suástegui JM
[Ad] Endereço:Centro de Investigaciones Biológicas del Noroeste, Av. Instituto Politécnico Nacional 195, 23096 La Paz, Baja California Sur, Mexico.
[Ti] Título:Digestive enzymes of the Californian two-spot octopus, Octopus bimaculoides (Pickford and McConnaughey, 1949).
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;215:10-18, 2018 Jan.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Octopus bimaculoides is an important commercially fished species in the California Peninsula with aquaculture potential; however, to date limited information is available regarding its digestive physiology. The objective of this study was focused on biochemically characterizing the main enzymes involved in the digestion of O. bimaculoides. Optimum pH, temperature and thermostability were determined for amylases, lipases, trypsin and chymotrypsin; optimum pH and protease inhibitor effect were assessed for acidic and alkaline proteases, and the effect of divalent ions on trypsin and chymotrypsin activity was evaluated in enzymatic extracts from the digestive (DG) and salivary glands (SG) and crop gastric juices (GJ). High amylase activity was detected in GD and GJ whereas this activity is very low in other cephalopods. Salivary glands had the greatest activity in most of the enzyme groups, showing the importance of this organ in digestion. Optimum pH was different depending on the organ and enzyme analyzed. The optimum pH in DG was 3 showing the predominance of acidic proteases in the digestion process. All enzymes were resistant and stable at high temperatures in contrast with other marine species. Trypsin and chymotrypsin activity were highly incremented with the presence of Mg , Co , Cu and Zn in some tissues. The inhibitor assay showed the importance of serine proteases, metalloproteases and aspartic proteases in the digestive process of this species. This study is the first in assessing the main digestive enzymes of O. bimaculoides and in remarking the importance of other digestive enzyme groups besides proteases in octopuses.
[Mh] Termos MeSH primário: Amilases/metabolismo
Quimotripsina/metabolismo
Lipase/metabolismo
Octopodiformes/metabolismo
Tripsina/metabolismo
[Mh] Termos MeSH secundário: Animais
Suco Gástrico/enzimologia
Glândulas Salivares/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.1.3 (Lipase); EC 3.2.1.- (Amylases); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171201
[Lr] Data última revisão:
171201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171029
[St] Status:MEDLINE


  3 / 12942 MEDLINE  
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[PMID]:28843429
[Au] Autor:Grille Coronel L; Acierno JP; Ermácora MR
[Ad] Endereço:Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Pena 352, B1876BXD Bernal, Pcia. de Buenos Aires, Argentina.
[Ti] Título:Ultracompact states of native proteins.
[So] Source:Biophys Chem;230:36-44, 2017 Nov.
[Is] ISSN:1873-4200
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A statistical analysis of circa 20,000 X-ray structures evidenced the effects of temperature of data collection on protein intramolecular distances and degree of compaction. Identical chains with data collected at cryogenic ultralow temperatures (≤160K) showed a radius of gyration (R ) significantly smaller than at moderate temperatures (≥240K). Furthermore, the analysis revealed the existence of structures with a R significantly smaller than expected for cryogenic temperatures. In these ultracompact cases, the unusually small R could not be specifically attributed to any experimental parameter or crystal features. Ultracompaction involves most atoms and results in their displacement toward the center of the molecule. Ultracompact structures on average have significantly shorter van der Waals and hydrogen bonds than expected for ultralow temperature structures. In addition, the number of van der Waals contacts was larger in ultracompact than in ultralow temperature structures. The structure of these ultracompact states was analyzed in detail and the implication and possible causes of the phenomenon are discussed.
[Mh] Termos MeSH primário: Proteínas/química
[Mh] Termos MeSH secundário: Animais
Bovinos
Quimotripsina/química
Ciclinas/química
Bases de Dados de Proteínas
Fator VII/química
Antígenos HLA-DR/química
Seres Humanos
Ligações de Hidrogênio
Estrutura Terciária de Proteína
Eletricidade Estática
Temperatura Ambiente
Tripsina/química
Microglobulina-2 beta/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclins); 0 (HLA-DR Antigens); 0 (Proteins); 0 (beta 2-Microglobulin); 9001-25-6 (Factor VII); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.1 (alpha-chymotrypsin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status:MEDLINE


  4 / 12942 MEDLINE  
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[PMID]:28841794
[Au] Autor:Lee H; Park Y; Kim S
[Ad] Endereço:Department of Chemistry, Seoul National University , Seoul 08826, Republic of Korea.
[Ti] Título:Enzymatic Cross-Linking of Side Chains Generates a Modified Peptide with Four Hairpin-like Bicyclic Repeats.
[So] Source:Biochemistry;56(37):4927-4930, 2017 Sep 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Macrocyclization of peptides is often employed to generate novel structures and biological activities in the biosynthesis of natural products and drug discovery. The enzymatic cross-linking of two side chains in a peptide via an ester or amide has a high potential for making topologically diverse cyclic peptides but is found with only a single consensus sequence in the microviridin class of natural products. Here, we report that a peptide with a new sequence pattern can be enzymatically cross-linked to make a novel microviridin-like peptide, plesiocin, which contains four repeats of a distinct hairpin-like bicyclic structure and shows strong inhibition of proteases. A single ATP-grasp enzyme binds to a leader peptide, of which only 13 residues are required for binding, and performs eight esterification reactions on the core peptide. We also demonstrate that the combination of tandem mass spectrometry and an ester-specific reaction greatly facilitates the determination of connectivity. We suggest that the enzymatic cross-linking of peptide side chains can generate more diverse structures in nature or by engineering.
[Mh] Termos MeSH primário: Organismos Aquáticos/metabolismo
Desenho de Drogas
Myxococcales/metabolismo
Peptídeos Cíclicos/metabolismo
Peptídeos/metabolismo
Inibidores de Proteases/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Organismos Aquáticos/enzimologia
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Proteínas de Bactérias/farmacologia
Cromatografia Líquida de Alta Pressão
Quimotripsina/antagonistas & inibidores
Quimotripsina/metabolismo
Esterificação
Interações Hidrofóbicas e Hidrofílicas
Sequências Repetidas Invertidas
Cinética
Estrutura Molecular
Família Multigênica
Myxococcales/enzimologia
Elastase Pancreática/antagonistas & inibidores
Elastase Pancreática/metabolismo
Peptídeos/química
Peptídeos/farmacologia
Peptídeos Cíclicos/química
Peptídeos Cíclicos/farmacologia
Inibidores de Proteases/química
Inibidores de Proteases/farmacologia
Conformação Proteica
Proteólise/efeitos dos fármacos
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Peptides); 0 (Peptides, Cyclic); 0 (Protease Inhibitors); 0 (plesiocin); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.36 (Pancreatic Elastase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00808


  5 / 12942 MEDLINE  
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[PMID]:28800614
[Au] Autor:Vatanparast M; Kim Y
[Ad] Endereço:Department of Plant Protection, College of Agriculture, University of Bu-Ali Sina, Hamedan, Iran.
[Ti] Título:Optimization of recombinant bacteria expressing dsRNA to enhance insecticidal activity against a lepidopteran insect, Spodoptera exigua.
[So] Source:PLoS One;12(8):e0183054, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Double-stranded RNA (dsRNA) has been applied to control insect pests due to its induction of RNA interference (RNAi) of a specific target gene expression. However, developing dsRNA-based insecticidal agent has been a great challenge especially against lepidopteran insect pests due to variations in RNAi efficiency. The objective of this study was to screen genes of chymotrypsins (SeCHYs) essential for the survival of the beet armyworm, Spodoptera exigua, to construct insecticidal dsRNA. In addition, an optimal oral delivery method was developed using recombinant bacteria. At least 7 SeCHY genes were predicted from S. exigua transcriptomes. Subsequent analyses indicated that SeCHY2 was widely expressed in different developmental stages and larval tissues by RT-PCR and its expression knockdown by RNAi caused high mortality along with immunosuppression. However, a large amount of dsRNA was required to efficiently kill late instars of S. exigua because of high RNase activity in their midgut lumen. To minimize dsRNA degradation, bacterial expression and formulation of dsRNA were performed in HT115 Escherichia coli using L4440 expression vector. dsRNA (300 bp) specific to SeCHY2 overexpressed in E. coli was toxic to S. exigua larvae after oral administration. To enhance dsRNA release from E. coli, bacterial cells were sonicated before oral administration. RNAi efficiency of sonicated bacteria was significantly increased, causing higher larval mortality at oral administration. Moreover, targeting young larvae possessing weak RNase activity in the midgut lumen significantly enhanced RNAi efficiency and subsequent insecticidal activity against S. exigua.
[Mh] Termos MeSH primário: Agentes de Controle Biológico/metabolismo
Quimotripsina/antagonistas & inibidores
Proteínas de Insetos/antagonistas & inibidores
Larva/genética
RNA de Cadeia Dupla/genética
Spodoptera/genética
[Mh] Termos MeSH secundário: Administração Oral
Animais
Quimotripsina/genética
Quimotripsina/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Regulação da Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Proteínas de Insetos/genética
Proteínas de Insetos/metabolismo
Larva/crescimento & desenvolvimento
Larva/metabolismo
Controle Biológico de Vetores/métodos
Filogenia
Isoformas de Proteínas/antagonistas & inibidores
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
RNA de Cadeia Dupla/metabolismo
Sonicação
Spodoptera/classificação
Spodoptera/crescimento & desenvolvimento
Spodoptera/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Control Agents); 0 (Insect Proteins); 0 (Protein Isoforms); 0 (RNA, Double-Stranded); EC 3.4.21.1 (Chymotrypsin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183054


  6 / 12942 MEDLINE  
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[PMID]:28700204
[Au] Autor:Chiba F; Twyman LJ
[Ad] Endereço:Department of Chemistry, University of Sheffield , Dainton Building, Brook Hill, Sheffield, South Yorkshire S3 7HF, United Kingdom.
[Ti] Título:Effect of Terminal-Group Functionality on the Ability of Dendrimers to Bind Proteins.
[So] Source:Bioconjug Chem;28(8):2046-2050, 2017 Aug 16.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is known that dendrimers can bind proteins with good selectively. This selectivity comes about from an optimization based on matching the size of the dendrimer with the size of the protein's interfacial binding area. In this paper, we report how this selectivity can be moderated by the functionality on the surface of the dendrimer. Specifically, we describe the synthesis of amino acid functionalized dendrimers and the effect of functionality on the dendrimer's ability to bind and inhibit the enzymatic protein, chymotrypsin. The results show how dendrimer binding can be increased or decreased depending on the terminal functionality. These results will allow new ligands to be designed and synthesized, possessing increased and selective protein-binding abilities.
[Mh] Termos MeSH primário: Quimotripsina/metabolismo
Dendrímeros/química
Dendrímeros/metabolismo
[Mh] Termos MeSH secundário: Ligação Proteica
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dendrimers); EC 3.4.21.1 (Chymotrypsin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00350


  7 / 12942 MEDLINE  
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[PMID]:28653909
[Au] Autor:Siddiqui SZ; Zahid A; Abbasi MA; Rehman A; Nasim FH
[Ad] Endereço:Department of Chemistry, Government College University, Lahore, Pakistan.
[Ti] Título:Synthetic N-[(substitutedsulfamoyl)phenyl]acetamides as moderate chymotrypsin inhibitors.
[So] Source:Pak J Pharm Sci;30(3):675-681, 2017 May.
[Is] ISSN:1011-601X
[Cp] País de publicação:Pakistan
[La] Idioma:eng
[Ab] Resumo:A facile method has been implemented for the synthesis of different N-substituted sulfamoylacetamides by reacting 4-acetamidobenzenesulfonyl chloride (1) with different alkyl/aralkyl/aryl amines (2a-q) in basic aqueous media under controlled pH to afford -[(Substitutedsulfamoyl) phenyl]acetamides (3a-q) which were confirmed through spectral analysis like FT-IR, EIMS and H-NMR. Moreover, the synthesized derivatives were screened against α-Chymotrypsin. The enzyme inhibitory results revealed that most of the synthesized compounds were found to be moderate enzyme inhibitors.
[Mh] Termos MeSH primário: Acetamidas/farmacologia
Quimotripsina/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
[Mh] Termos MeSH secundário: Acetamidas/química
Inibidores Enzimáticos/química
Espectroscopia de Prótons por Ressonância Magnética
Espectrometria de Massas por Ionização por Electrospray
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetamides); 0 (Enzyme Inhibitors); EC 3.4.21.1 (Chymotrypsin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


  8 / 12942 MEDLINE  
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[PMID]:28612358
[Au] Autor:Sirotkin VA; Kuchierskaya AA
[Ad] Endereço:Department of Physical Chemistry, Kazan Federal University, A.M. Butlerov Institute of Chemistry, Kazan, 420008, Russia.
[Ti] Título:α-chymotrypsin in water-acetone and water-dimethyl sulfoxide mixtures: Effect of preferential solvation and hydration.
[So] Source:Proteins;85(10):1808-1819, 2017 Oct.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We investigated water/organic solvent sorption and residual enzyme activity to simultaneously monitor preferential solvation/hydration of protein macromolecules in the entire range of water content at 25°C. We applied this approach to estimate protein destabilization/stabilization due to the preferential interactions of bovine pancreatic α-chymotrypsin with water-acetone (moderate-strength H-bond acceptor) and water-DMSO (strong H-bond acceptor) mixtures. There are three concentration regimes for the dried α-chymotrypsin. α-Chymotrypsin is preferentially hydrated at high water content. The residual enzyme activity values are close to 100%. At intermediate water content, the dehydrated α-chymotrypsin has a higher affinity for acetone/DMSO than for water. Residual enzyme activity is minimal in this concentration range. The acetone/DMSO molecules are preferentially excluded from the protein surface at the lowest water content, resulting in preferential hydration. The residual catalytic activity in the water-poor acetone is ∼80%, compared with that observed after incubation in pure water. This effect is very small for the water-poor DMSO. Two different schemes are operative for the hydrated enzyme. At high and intermediate water content, α-chymotrypsin exhibits preferential hydration. However, at intermediate water content, in contrast to the dried enzyme, the initially hydrated α-chymotrypsin possesses increased preferential hydration parameters. At low water content, no residual enzyme activity was observed. Preferential binding of DMSO/acetone to α-chymotrypsin was detected. Our data clearly demonstrate that the hydrogen bond accepting ability of organic solvents and the protein hydration level constitute key factors in determining the stability of protein-water-organic solvent systems.
[Mh] Termos MeSH primário: Quimotripsina/química
Conformação Proteica
Solventes/química
Água/química
[Mh] Termos MeSH secundário: Acetona
Dimetil Sulfóxido/química
Ligações de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Solvents); 059QF0KO0R (Water); 1364PS73AF (Acetone); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.1 (alpha-chymotrypsin); YOW8V9698H (Dimethyl Sulfoxide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25334


  9 / 12942 MEDLINE  
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[PMID]:28589736
[Au] Autor:Zupancic O; Rohrer J; Thanh Lam H; Grießinger JA; Bernkop-Schnürch A
[Ad] Endereço:a Department of Pharmaceutical Technology, Institute of Pharmacy , Leopold-Franzens-University Innsbruck , Innsbruck , Austria.
[Ti] Título:Development and in vitro characterization of self-emulsifying drug delivery system (SEDDS) for oral opioid peptide delivery.
[So] Source:Drug Dev Ind Pharm;43(10):1694-1702, 2017 Oct.
[Is] ISSN:1520-5762
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: In this study, self-emulsifying drug delivery system (SEDDS) for oral delivery of opioid peptide dalargin were developed and characterized in vitro. METHODS: Dalargin lipophilicity was increased by O-esterification of tyrosine OH group, hydrophobic ion pairing, or a combination thereof. Distribution coefficients (log D) of lipidized dalargin derivatives were determined. Then, dalargin was incorporated in chosen SEDDS, namely SEDDS-1, composed of 50% Capmul 907, 40% Cremophor EL, and 10% propylene glycol and comparatively more lipophilic SEDDS-2 composed of 30% Captex 8000, 30% Capmul MCM, 30% Cremophor EL, and 10% propylene glycol. Additionally, SEDDS were characterized regarding droplet size, polydispersity index (PDI), cloudy point, physical stability and stability against pancreatic lipase. Furthermore, mucus permeating properties of SEDDS and their ability to protect the incorporated dalargin against proteolysis by trypsin, α-chymotrypsin, elastase, simulated gastric fluid (SGF), and simulated intestinal fluid (SIF) were evaluated. RESULTS: The highest dalargin drug payload of 4.57% in SEDDS-2 was achieved when dalargin palmitate (pDAL) was ion paired with sodium dodecyl sulfate (SDS) in molar ratio 1:1. Moreover, SEDDS-1 and SEDDS-2 had a narrow droplet size distribution with average droplet sizes of 42.1 and 33.1 nm with PDI of 0.042 and 0.034, respectively. Lipolysis study showed that within 30 min 78.5% of SEDDS-1 and 92.1% of SEDDS-2 were digested. In addition, both SEDDS exhibited mucus permeating properties as well as a protective effect against enzymatic degradation by trypsin, α-chymotrypsin, elastase, SGF and SIF. CONCLUSION: The results of this study suggest that the developed SEDDS could be considered for oral opioid peptide delivery.
[Mh] Termos MeSH primário: Caprilatos/química
Quimotripsina/química
Sistemas de Liberação de Medicamentos/métodos
Emulsões/química
Glicerídeos/química
Lipídeos/química
Muco/química
Peptídeos Opioides/química
Polietilenoglicóis/química
Propilenoglicol/química
[Mh] Termos MeSH secundário: Administração Oral
Disponibilidade Biológica
Peptídeos Opioides/administração & dosagem
Peptídeos Opioides/farmacologia
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caprylates); 0 (Emulsions); 0 (Glycerides); 0 (Lipids); 0 (Opioid Peptides); 30IQX730WE (Polyethylene Glycols); 39279-69-1 (cremophor); 6DC9Q167V3 (Propylene Glycol); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.1 (alpha-chymotrypsin); VFU0OU98LO (monooctanoin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1080/03639045.2017.1338722


  10 / 12942 MEDLINE  
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[PMID]:28551252
[Au] Autor:Colgrave ML; Byrne K; Howitt CA
[Ad] Endereço:CSIRO Agriculture and Food, 306 Carmody Rd, St Lucia, QLD 4067, Australia. Electronic address: michelle.colgrave@csiro.au.
[Ti] Título:Food for thought: Selecting the right enzyme for the digestion of gluten.
[So] Source:Food Chem;234:389-397, 2017 Nov 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gluten describes a complex mixture of proteins found in wheat, rye, barley and oats that pose a health risk to people affected by conditions such as coeliac disease and non-coeliac gluten sensitivity. Complete digestion of gluten proteins is of critical importance during quantitative analysis. To this end, chymotrypsin was investigated for its ability to efficiently and reproducibly digest specific classes of gluten in barley. Using proteomics a chymotryptic peptide marker panel was elucidated and subjected to relative quantification using LC-MRM-MS. Thorough investigation of peptide markers revealed robust and reproducible quantification with CVs <15% was possible, however a greater proportion of non-specific cleavage variants were observed relative to trypsin. The selected peptide markers were assessed to ensure their efficient liberation from their parent proteins. While trypsin remains the preferred enzyme for quantification of the avenin-like A proteins, the B-, D- and γ-hordeins, chymotrypsin was the enzyme of choice for the C-hordeins.
[Mh] Termos MeSH primário: Quimotripsina/química
Glutens/química
Hordeum/química
Tripsina/química
[Mh] Termos MeSH secundário: Cromatografia Líquida
Espectrometria de Massas
Prolaminas/química
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Prolamins); 8002-80-0 (Glutens); EC 3.4.21.1 (Chymotrypsin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE



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