Base de dados : MEDLINE
Pesquisa : D12.776.860 [Categoria DeCS]
Referências encontradas : 16 [refinar]
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  1 / 16 MEDLINE  
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[PMID]:28480388
[Au] Autor:Togun RA; Balogun RO; Adeyemi DO; Esan TA; Oyatogun GM; Oziegbe EO; Okonji RE; Kuku A
[Ad] Endereço:Department of Haematology and Immunology, Faculty of Basic Medical Sciences, Obafemi Awolowo University, Ile-Ife, Nigeria.
[Ti] Título:ISOLATION, CHARACTERIZATION AND IMMUNOCHEMICAL STUDIES ON FIBROUS PROTEINS FROM COWRY SHELL , LINNAEUS).
[So] Source:Afr J Tradit Complement Altern Med;14(1):110-122, 2017.
[Is] ISSN:2505-0044
[Cp] País de publicação:Nigeria
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Biomaterials are non-drug substances used to treat, enhance or replace functions of body tissues or organs. Natural sources of biomaterials have recently become the focus of several research activities. Cowry shell constitutes one of the most promising natural sources of biomaterials because of its chemical stability, biodegradability and biocompatibility in the body. However, its applications may be limited due to immunogenic and toxic responses that may occur following implantation, hence this study. MATERIALS AND METHODS: Crude fibrous protein extracted with citrate buffer from pulverised cowry shells ( (L)), was resolved into two components (CSP1 and CSP2) by gel filtration. Immunological studies were performed with antisera obtained from rabbits by double immunodiffusion and immunoelectrophoresis techniques. Mice treated with the proteins were observed for signs of toxicity and their liver, kidney, lungs and spleen were processed histologically. RESULTS: The native molecular weight of CSP1 and CSP2 determined by gel filtration were 91kDa and 33kDa respectively. CSP1 and CSP2 displayed single bands on SDS-PAGE with subunit molecular weight values of 19kDa and 19.5kDa respectively. Antisera obtained from rabbits immunised with the crude citrate buffer extracts precipitated the antigen in double immunodiffusion tests. Histopathological examinations revealed a dose-dependent damaging effect of the shell proteins on liver, kidney, lung and spleen tissues of the treated mice. CONCLUSION: This study showed that cowry shells contain fibrous proteins which are immunogenic and toxic in mice at relatively high concentrations, causing visible organ damage without concurrent physical manifestations.
[Mh] Termos MeSH primário: Exoesqueleto/química
Fatores Imunológicos/química
Fatores Imunológicos/isolamento & purificação
Escleroproteínas/química
Escleroproteínas/isolamento & purificação
Caramujos/química
[Mh] Termos MeSH secundário: Animais
Fatores Imunológicos/efeitos adversos
Fatores Imunológicos/farmacologia
Rim/efeitos dos fármacos
Fígado/efeitos dos fármacos
Camundongos
Peso Molecular
Coelhos
Escleroproteínas/efeitos adversos
Escleroproteínas/farmacologia
Pele/efeitos dos fármacos
Baço/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunologic Factors); 0 (Scleroproteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.21010/ajtcam.v14i1.12


  2 / 16 MEDLINE  
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[PMID]:28101857
[Au] Autor:Squire JM; Parry DA
[Ad] Endereço:Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK. j.squire@imperial.ac.uk.
[Ti] Título:Fibrous Protein Structures: Hierarchy, History and Heroes.
[So] Source:Subcell Biochem;82:1-33, 2017.
[Is] ISSN:0306-0225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During the 1930s and 1940s the technique of X-ray diffraction was applied widely by William Astbury and his colleagues to a number of naturally-occurring fibrous materials. On the basis of the diffraction patterns obtained, he observed that the structure of each of the fibres was dominated by one of a small number of different types of molecular conformation. One group of fibres, known as the k-m-e-f group of proteins (keratin - myosin - epidermin - fibrinogen), gave rise to diffraction characteristics that became known as the α-pattern. Others, such as those from a number of silks, gave rise to a different pattern - the ß-pattern, while connective tissues yielded a third unique set of diffraction characteristics. At the time of Astbury's work, the structures of these materials were unknown, though the spacings of the main X-ray reflections gave an idea of the axial repeats and the lateral packing distances. In a breakthrough in the early 1950s, the basic structures of all of these fibrous proteins were determined. It was found that the long protein chains, composed of strings of amino acids, could be folded up in a systematic manner to generate a limited number of structures that were consistent with the X-ray data. The most important of these were known as the α-helix, the ß-sheet, and the collagen triple helix. These studies provided information about the basic building blocks of all proteins, both fibrous and globular. They did not, however, provide detailed information about how these molecules packed together in three-dimensions to generate the fibres found in vivo. A number of possible packing arrangements were subsequently deduced from the X-ray diffraction and other data, but it is only in the last few years, through the continued improvements of electron microscopy, that the packing details within some fibrous proteins can now be seen directly. Here we outline briefly some of the milestones in fibrous protein structure determination, the role of the amino acid sequences and how new techniques, including electron microscopy, are helping to define fibrous protein structures in three-dimensions. We also introduce the idea that, from the known sequence characteristics of different fibrous proteins, new molecules can be designed and synthesized, thereby generating new biological materials with specific structural properties. Some of these, for example, are planned for use in drug delivery systems. Along the way we also introduce the various Chapters of the book, where individual fibrous proteins are discussed in detail.
[Mh] Termos MeSH primário: Estrutura Secundária de Proteína
Escleroproteínas/química
[Mh] Termos MeSH secundário: Aminoácidos/química
Animais
Cristalografia por Raios X/história
Cristalografia por Raios X/métodos
História do Século XX
História do Século XXI
Seres Humanos
Modelos Moleculares
[Pt] Tipo de publicação:HISTORICAL ARTICLE; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Amino Acids); 0 (Scleroproteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-49674-0_1


  3 / 16 MEDLINE  
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[PMID]:28034822
[Au] Autor:Thiruselvi T; Thirupathi Kumara Raja S; Shanuja SK; Iswarya S; Gnanamani A
[Ad] Endereço:CSIR-Central Leather Research Institute, Adyar, Chennai 20, Tamil Nadu, India.
[Ti] Título:Induced oxidative stress management in wounds through phenolic acids engineered fibrous protein: An in vitro assessment using polymorphonuclear (PMN) cells.
[So] Source:Int J Biol Macromol;96:485-493, 2017 Mar.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The present study explores the preparation, characterization and the role of phenolic acid tethered fibrous protein in the management of induced oxidative stress studied under in vitro conditions. In brief, the biomaterial is prepared by engineering the fibrous protein with dihydroxy and trihydroxy phenolic acid moieties and subjected to characterization to ensure the tethering. The resultant biomaterial studied for its efficacy as a free radical scavenger using polymorphonuclear (PMN) cells with induced oxidative stress and also as an agent for cell migration using fibroblasts cells. Results revealed that induced oxidative stress in PMN cells after exposure to UVB radiation managed well with the prepared biomaterial by reducing the levels of superoxide anion, oxygen and hydroxyl radicals. Further, the protein and the phenolic acid interaction supports the cell migration as evidenced from the scratch assay. In conclusion, though phenolic acids are well known for their antimicrobial and antioxidant potential, indenting these acids directly to the wounds is not sensible, but tethering to protein explored the scavenging activity as expected. The present study infers that phenolic acid engineered protein has a significant role in managing the imbalance in the redox state prevailing in wounds and supports the healing at appreciable level.
[Mh] Termos MeSH primário: Hidroxibenzoatos/química
Hidroxibenzoatos/farmacologia
Neutrófilos/efeitos dos fármacos
Neutrófilos/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Escleroproteínas/química
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Antioxidantes/farmacologia
Compostos de Bifenilo/metabolismo
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Espaço Extracelular/efeitos dos fármacos
Espaço Extracelular/metabolismo
Espaço Extracelular/efeitos da radiação
Radical Hidroxila/metabolismo
Metaloproteinases da Matriz/metabolismo
Neutrófilos/citologia
Neutrófilos/efeitos da radiação
Estresse Oxidativo/efeitos da radiação
Picratos/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Superóxidos/metabolismo
Suínos
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biphenyl Compounds); 0 (Hydroxybenzoates); 0 (Picrates); 0 (Reactive Oxygen Species); 0 (Scleroproteins); 11062-77-4 (Superoxides); 29656-58-4 (phenolic acid); 3352-57-6 (Hydroxyl Radical); DFD3H4VGDH (1,1-diphenyl-2-picrylhydrazyl); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161231
[St] Status:MEDLINE


  4 / 16 MEDLINE  
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[PMID]:26784838
[Au] Autor:Chang EP; Perovic I; Rao A; Cölfen H; Evans JS
[Ad] Endereço:Laboratory for Chemical Physics, Division of Basic Sciences and Center for Skeletal Biology, New York University , 345 E. 24th Street, New York, New York 10010, United States.
[Ti] Título:Insect Cell Glycosylation and Its Impact on the Functionality of a Recombinant Intracrystalline Nacre Protein, AP24.
[So] Source:Biochemistry;55(7):1024-35, 2016 Feb 23.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The impacts of glycosylation on biomineralization protein function are largely unknown. This is certainly true for the mollusk shell, where glycosylated intracrystalline proteins such as AP24 (Haliotis rufescens) exist but their functions and the role of glycosylation remain elusive. To assess the effect of glycosylation on protein function, we expressed two recombinant variants of AP24: an unglycosylated bacteria-expressed version (rAP24N) and a glycosylated insect cell-expressed version (rAP24G). Our findings indicate that rAP24G is expressed as a single polypeptide containing variations in glycosylation that create microheterogeneity in rAP24G molecular masses. These post-translational modifications incorporate O- and N-glycans and anionic monosialylated and bisialylated, and monosulfated and bisulfated monosaccharides on the protein molecules. AFM and DLS experiments confirm that both rAP24N and rAP24G aggregate to form protein phases, with rAP24N exhibiting a higher degree of aggregation, compared to rAP24G. With regard to functionality, we observe that both recombinant proteins exhibit similar behavior within in vitro calcium carbonate mineralization assays and potentiometric titrations. However, rAP24G modifies crystal growth directions and is a stronger nucleation inhibitor, whereas rAP24N exhibits higher mineral phase stabilization and nanoparticle containment. We believe that the post-translational addition of anionic groups (via sialylation and sulfation), along with modifications to the protein surface topology, may explain the changes in glycosylated rAP24G aggregation and mineralization behavior, relative to rAP24N.
[Mh] Termos MeSH primário: Gastrópodes/química
Glicoproteínas/química
Nácar/química
Processamento de Proteína Pós-Traducional
Escleroproteínas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Calcificação Fisiológica
Biologia Computacional
Escherichia coli
Gastrópodes/ultraestrutura
Glicoproteínas/genética
Glicoproteínas/metabolismo
Glicosilação
Microscopia Eletrônica de Varredura
Microscopia Eletrônica de Transmissão
Dados de Sequência Molecular
Peso Molecular
Polissacarídeos/química
Polissacarídeos/metabolismo
Agregados Proteicos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Escleroproteínas/genética
Escleroproteínas/metabolismo
Células Sf9
Spodoptera
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Nacre); 0 (Polysaccharides); 0 (Protein Aggregates); 0 (Recombinant Proteins); 0 (Scleroproteins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170905
[Lr] Data última revisão:
170905
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160120
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.5b01186


  5 / 16 MEDLINE  
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[PMID]:26332660
[Au] Autor:Yigit S; Dinjaski N; Kaplan DL
[Ad] Endereço:Department of Biomedical Engineering, Tufts University, Medford, Massachusetts, 02155.
[Ti] Título:Fibrous proteins: At the crossroads of genetic engineering and biotechnological applications.
[So] Source:Biotechnol Bioeng;113(5):913-29, 2016 May.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fibrous proteins, such as silk, elastin and collagen are finding broad impact in biomaterial systems for a range of biomedical and industrial applications. Some of the key advantages of biosynthetic fibrous proteins compared to synthetic polymers include the tailorability of sequence, protein size, degradation pattern, and mechanical properties. Recombinant DNA production and precise control over genetic sequence of these proteins allows expansion and fine tuning of material properties to meet the needs for specific applications. We review current approaches in the design, cloning, and expression of fibrous proteins, with a focus on strategies utilized to meet the challenges of repetitive fibrous protein production. We discuss recent advances in understanding the fundamental basis of structure-function relationships and the designs that foster fibrous protein self-assembly towards predictable architectures and properties for a range of applications. We highlight the potential of functionalization through genetic engineering to design fibrous protein systems for biotechnological and biomedical applications.
[Mh] Termos MeSH primário: Biotecnologia/métodos
Clonagem Molecular/métodos
Engenharia de Proteínas/métodos
Escleroproteínas/genética
Seda/genética
[Mh] Termos MeSH secundário: Animais
Colágeno/química
Colágeno/genética
Colágeno/isolamento & purificação
Colágeno/metabolismo
Elastina/química
Elastina/genética
Elastina/isolamento & purificação
Elastina/metabolismo
Seres Humanos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Escleroproteínas/química
Escleroproteínas/isolamento & purificação
Escleroproteínas/metabolismo
Seda/química
Seda/isolamento & purificação
Seda/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (Scleroproteins); 0 (Silk); 9007-34-5 (Collagen); 9007-58-3 (Elastin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150903
[St] Status:MEDLINE
[do] DOI:10.1002/bit.25820


  6 / 16 MEDLINE  
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[PMID]:24875424
[Au] Autor:Parry DA
[Ad] Endereço:Massey University, Institute of Fundamental Sciences, College of Sciences, Private Bag 11-222, Palmerston North, New Zealand. Electronic address: d.parry@massey.ac.nz.
[Ti] Título:Alpbach special issue.
[So] Source:J Struct Biol;186(3):319, 2014 Jun.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Escleroproteínas/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
História do Século XX
Conformação Proteica
Escleroproteínas/metabolismo
[Pt] Tipo de publicação:EDITORIAL; HISTORICAL ARTICLE
[Nm] Nome de substância:
0 (Scleroproteins)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:140530
[Lr] Data última revisão:
140530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140531
[St] Status:MEDLINE


  7 / 16 MEDLINE  
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[PMID]:24476562
[Au] Autor:Witherspoon JW; Smirnova IV; McIff TE
[Ad] Endereço:Department of Physical Therapy and Rehabilitation Science, University of Kansas Medical Center , Kansas City, Kansas.
[Ti] Título:Improved gold chloride staining method for anatomical analysis of sensory nerve endings in the shoulder capsule and labrum as examples of loose and dense fibrous tissues.
[So] Source:Biotech Histochem;89(5):355-70, 2014 Jul.
[Is] ISSN:1473-7760
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Consistency in gold chloride staining is essential for anatomical analysis of sensory nerve endings. The gold chloride stain for this purpose has been modified by many investigators, but often yields inconsistent staining, which makes it difficult to differentiate structures and to determine nerve ending distribution in large tissue samples. We introduce additional steps and major changes to the modified Gairns' protocol. We controlled the temperature and mixing rate during tissue staining to achieve consistent staining and complete solution penetration. We subjected samples to sucrose dehydration to improve cutting efficiency. We then exposed samples to a solution containing lemon juice, formic acid and paraformaldehyde to produce optimal tissue transparency with minimal tissue deformity. We extended the time for gold chloride impregnation 1.5 fold. Gold chloride was reduced in the labrum using 25% formic acid in water for 18 h and in the capsule using 25% formic acid in citrate phosphate buffer for 2 h. Citrate binds gold nanoparticles, which minimizes aggregation in the tissue. We stored samples in fresh ultrapure water at 4° C to slow reduction and to maintain color contrast in the tissue. Tissue samples were embedded in Tissue Tek and sectioned at 80 and 100 µm instead of using glycerin and teasing the tissue apart as in Gairns' modified gold chloride method. We attached sections directly to gelatin subbed slides after sectioning with a cryostat. The slides then were processed and coverslipped with Permount. Staining consistency was demonstrated throughout the tissue sections and neural structures were clearly identifiable.
[Mh] Termos MeSH primário: Compostos de Ouro/química
Células Receptoras Sensoriais/química
Coloração e Rotulagem
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
Meia-Idade
Escleroproteínas/química
Células Receptoras Sensoriais/citologia
Ombro/anatomia & histologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gold Compounds); 0 (Scleroproteins); 11118-27-7 (gold chloride)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140131
[St] Status:MEDLINE
[do] DOI:10.3109/10520295.2013.872297


  8 / 16 MEDLINE  
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[PMID]:24148884
[Au] Autor:Parry DA
[Ad] Endereço:Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North 4442, New Zealand. Electronic address: d.parry@massey.ac.nz.
[Ti] Título:Fifty years of fibrous protein research: a personal retrospective.
[So] Source:J Struct Biol;186(3):320-34, 2014 Jun.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As a result of X-ray fiber diffraction studies on fibrous proteins and crystallographic data on fragments derived from them, new experimental techniques across the biophysical and biochemical spectra, sophisticated computer modeling and refinement procedures, widespread use of bioinformatics and improved specimen preparative procedures the structures of many fibrous proteins have now been determined to at least low resolution. In so doing these structures have yielded insight into the relationship that exists between sequence and conformation and this, in turn, has led to improved methodologies for predicting structure from sequence data alone. In this personal retrospective a selection of progress made during the past 50years is discussed in terms of events to which the author has made some contribution.
[Mh] Termos MeSH primário: Pesquisa Biomédica/história
Escleroproteínas/química
[Mh] Termos MeSH secundário: Biofísica/métodos
Cristalografia por Raios X
História do Século XX
Queratinas/química
Modelos Moleculares
Plaquinas/química
Conformação Proteica
Tropomiosina/química
Difração de Raios X
[Pt] Tipo de publicação:HISTORICAL ARTICLE; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plakins); 0 (Scleroproteins); 0 (Tropomyosin); 68238-35-7 (Keratins)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:140530
[Lr] Data última revisão:
140530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131024
[St] Status:MEDLINE


  9 / 16 MEDLINE  
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[PMID]:23765989
[Au] Autor:Becker PM; Yu P
[Ad] Endereço:Wageningen UR Livestock Research, Lelystad, The Netherlands.
[Ti] Título:What makes protein indigestible from tissue-related, cellular, and molecular aspects?
[So] Source:Mol Nutr Food Res;57(10):1695-707, 2013 Oct.
[Is] ISSN:1613-4133
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:This paper gives an insight into key factors, which impair enzymatic protein digestion. By nature, some proteins in raw products are already poorly digestible because of structural peculiarities, or due to their occurrence in plant cytoplasmic organelles or in cell membranes. In plant-based protein, molecular and structural changes can be induced by genetic engineering, even if protein is not a target compound class of the genetic modification. Other proteins only become difficult to digest due to changes that occur during the processing of proteinaceous products, such as extruding, boiling, or acidic or alkaline treatment. The utilization of proteinaceous raw materials in industrial fermentations can also have negative impacts on protein digestibility, when reused as fermentation by-products for animal nutrition, such as brewers' grains. After consumption, protein digestion can be impeded in the intestine by the presence of antinutritional factors, which are ingested together with the food or feedstuff. It is concluded that the encircling matrix, but also molecular, chemical, and structural peculiarities or modifications to amino acids and proteins obstruct protein digestion by common proteolytic enzymes in humans and animals.
[Mh] Termos MeSH primário: Proteínas na Dieta/metabolismo
Digestão/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas na Dieta/química
Fermentação
Temperatura Alta
Seres Humanos
Concentração de Íons de Hidrogênio
Escleroproteínas/química
Proteínas de Armazenamento de Sementes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dietary Proteins); 0 (Scleroproteins); 0 (Seed Storage Proteins)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:131004
[Lr] Data última revisão:
131004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130615
[St] Status:MEDLINE
[do] DOI:10.1002/mnfr.201200592


  10 / 16 MEDLINE  
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[PMID]:23137042
[Au] Autor:Walker AA; Weisman S; Kameda T; Sutherland TD
[Ad] Endereço:Research School of Biology, Australian National University, Canberra, Australia, 0200.
[Ti] Título:Natural templates for coiled-coil biomaterials from praying mantis egg cases.
[So] Source:Biomacromolecules;13(12):4264-72, 2012 Dec 10.
[Is] ISSN:1526-4602
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Whereas there is growing interest in producing biomaterials containing coiled-coils, relatively few studies have made use of naturally occurring fibrous proteins. In this study, we have characterized fibrous proteins used by mother praying mantises to produce an extensive covering for their eggs called an ootheca and demonstrate the production of artificial ootheca using recombinantly produced proteins. Examination of natural oothecae by infrared spectroscopy and solid-state nuclear magnetic resonance revealed the material to consist of proteins organized predominately as coiled-coils. Two structural proteins, Mantis Fibroin 1 and Mantis Fibroin 2, were identified in ootheca from each of three species. Between species, the primary sequences of both proteins had diverged considerably, but other features were tightly conserved, including low molecular weight, high abundance of Ala, Glu, Lys, and Ser, and a triblock-like architecture with extensive central coiled-coil domain. Mantis fibroin hydrophobic cores had an unusual composition containing high levels of alanine and aromatic residues. Recombinantly produced mantis fibroins folded into coiled-coils in solution and could be fabricated into solid materials with high coiled-coil content. The structural features of mantis fibroins and their straightforward recombinant production make them promising templates for the production of coiled-coil biomimetics materials.
[Mh] Termos MeSH primário: Materiais Biocompatíveis/química
Materiais Biomiméticos/síntese química
Fibroínas/química
Mantódeos/química
Óvulo
[Mh] Termos MeSH secundário: Alanina/química
Sequência de Aminoácidos
Animais
Dicroísmo Circular
Escherichia coli/genética
Feminino
Fibroínas/genética
Biblioteca Gênica
Ácido Glutâmico/química
Interações Hidrofóbicas e Hidrofílicas
Lisina/química
Espectroscopia de Ressonância Magnética
Dados de Sequência Molecular
Peso Molecular
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Escleroproteínas/química
Alinhamento de Sequência
Análise de Sequência de DNA
Serina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biocompatible Materials); 0 (Recombinant Proteins); 0 (Scleroproteins); 3KX376GY7L (Glutamic Acid); 452VLY9402 (Serine); 9007-76-5 (Fibroins); K3Z4F929H6 (Lysine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121110
[St] Status:MEDLINE
[do] DOI:10.1021/bm301570v



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