Reverse micelles as hosts for proteins and small molecules

Luisi, Pier Luigi; Giomini, Marcello; Pileni, Marie‐Paule; Robinson, Brian H.

doi:10.1016/0304-4157(88)90025-1

Cited by 779 publications

(526 citation statements)

References 157 publications

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“…Most of the enzymes studied in the systems of reversed micelles exhibit a characteristic bell-shaped dependence of their catalytic activity on the degree of surfactant hydration [13][14][15][16][17]. Variations in this parameter are accompanied by changes in the size of the inner water cavity of reversed micelles [30,31].…”

Section: Resultsmentioning

confidence: 99%

“…Micellar enzymology is a novel approach to the study of the properties of biomolecules, and enzymes in particular. Its application reveals the enzyme's tendencies to form superactive conformations and supramolecular structures (reviewed in [13][14][15][16][17]). The results presented in this paper provide a new look into structure-function relationships in peroxidase catalysis.…”

Section: Introductionmentioning

confidence: 99%

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Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Gazaryan

Klyachko

Dulkis

et al. 1997

Biochemical Journal

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Wild-type recombinant horseradish peroxidase purified and refolded from Escherichia coli inclusion bodies has been studied in the system of bis(2-ethylhexyl)sulphosuccinate sodium salt (Aerosol OT)-reversed micelles in octane. In contrast with native horseradish peroxidase the wild-type recombinant enzyme forms dimeric structures as judged by sedimentation analysis. Peroxidase substrates affect the equilibrium between monomeric and dimeric enzyme forms. The dependence of the catalytic activity of recombinant peroxidase on the degree of hydration of the surfactant exhibits two maxima with pyrogallol, o-phenylene- diamine, guaiacol and o-dianisidine, with different ratios of activities for the first and second maxima. The differences in activities of monomeric and dimeric forms of the recombinant horseradish peroxidase provide evidence for active-site screening in dimeric forms. This has been used to model a dimeric structure of recombinant horseradish peroxidase with the screened entrance to the active site. In the model structure obtained, three of eight glycosylation sites were screened. This might explain the absence of dimeric structures in native enzyme peroxidase. The system of reversed micelles provides, for the first time, evidence for the formation of dimeric structures by recombinant plant peroxidase with an altered substrate specificity compared with the native enzyme. Thus one can assume that haem-containing peroxidases in general are able to form dimeric structures.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Gazaryan

Klyachko

Dulkis

et al. 1997

Biochemical Journal

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“…On the other hand, using organic solvents results in stronger affinities with the hydrophobic tails to form spheroidal aggregates which are structurally reverse of normal micelles, that is having an external shell of hydrophobic hydrocarbon chains and hydrophilic polar cores capable of solubilizing polar solvents. [113] In fact, such a reverse micelle (also named as microemulsion) is an isotropic dispersion of two immiscible liquids within a thermodynamically stable condition in which microdomain stabilization of either or both liquids is performed by an interfacial film of surfactant molecules. [92b] Eicke et al were the first to study the physical properties of the reverse micelles as water-in-oil (w/o) microemulsions in a comprehensive manner.…”

Section: Reverse Micelle (Microemulsion)mentioning

confidence: 99%

Synthesis, Functionalization, and Design of Magnetic Nanoparticles for Theranostic Applications

Mosayebi

Kiyasatfar

Laurent

2017

Adv Healthcare Materials

203

171

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In order to translate nanotechnology into medical practice, magnetic nanoparticles (MNPs) have been presented as a class of non‐invasive nanomaterials for numerous biomedical applications. In particular, MNPs have opened a door for simultaneous diagnosis and brisk treatment of diseases in the form of theranostic agents. This review highlights the recent advances in preparation and utilization of MNPs from the synthesis and functionalization steps to the final design consideration in evading the body immune system for therapeutic and diagnostic applications with addressing the most recent examples of the literature in each section. This study provides a conceptual framework of a wide range of synthetic routes classified mainly as wet chemistry, state‐of‐the‐art microfluidic reactors, and biogenic routes, along with the most popular coating materials to stabilize resultant MNPs. Additionally, key aspects of prolonging the half‐life of MNPs via overcoming the sequential biological barriers are covered through unraveling the biophysical interactions at the bio–nano interface and giving a set of criteria to efficiently modulate MNPs' physicochemical properties. Furthermore, concepts of passive and active targeting for successful cell internalization, by respectively exploiting the unique properties of cancers and novel targeting ligands are described in detail. Finally, this study extensively covers the recent developments in magnetic drug targeting and hyperthermia as therapeutic applications of MNPs. In addition, multi‐modal imaging via fusion of magnetic resonance imaging, and also innovative magnetic particle imaging with other imaging techniques for early diagnosis of diseases are extensively provided.

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“…Estas substâncias provavelmente foram muito comuns na Terra primitiva e diversas vantagens podem ser citadas em favor do mundo dos lipídios: estas moléculas se agrupam espontaneamente em complexas estruturas supramoleculares; estas estruturas supramoleculares podem agir como catalisadores e, contêm informação devido sua composição, podendo evoluir [54][55][56][57][58][59][60][61] . A polimerização de glicina dentro de vesículas de lipídios em hidrotermais foi estudada por Tsukahara et al 62 .…”

Section: Experimentos Não Envolvendo Mineraisunclassified

Adsorção de aminoácidos sobre minerais e a origem da vida

Zaia¹,

Zaia²

2006

Quím. Nova

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Recebido em 30/3/05; aceito em 15/7/05; publicado na web em 6/3/06 ADSORPTION OF AMINO ACIDS ON MINERALS AND THE ORIGIN OF LIFE. Minerals adsorb more readily amino acids with charged R groups than those with uncharged R groups, so that the incorporation of amino acids with charged R groups into peptides would be more frequent than that of amino acids with uncharged R groups. However, 74% of the amino acids in the proteins of modern organisms contain uncharged R groups. Thus, what could have been the mechanism that produced peptides/ proteins with more amino acids with uncharged R groups than precursors with charged R groups? The lipid world offers an alternative view of the origin of life. In the present paper, several other mechanisms are also discussed.Keywords: adsorption; minerals; amino acids. INTRODUÇÃOPodemos dizer que a grande maioria das reações químicas, que ocorrem em todos os seres vivos do nosso planeta, de alguma forma envolve proteínas e peptídeos e, em alguns casos, aminoácidos 1 . Por este motivo, a questão da formação de aminoácidos na Terra primitiva e sua condensação para peptídeos é um assunto extremamente importante para a química prebiótica. Neste artigo vamos partir do pressuposto que aminoácidos existiam em uma quantidade razoável na Terra primitiva. Podemos considerar, com uma boa margem de segurança, que esta suposição esteja correta visto que aminoácidos são facilmente sintetizados em diversos ambientes da química prebiótica, tais como mistura gasosas tanto de atmosferas redutoras como oxidantes 2-5 ; reações em estado sólido 6 ; reações simulando fontes hidrotermais ou em meio aquoso [7][8][9][10][11] . Também devemos lembrar que cometas e meteoros podem ter contribuído com uma parcela dos aminoácidos existentes na Terra primitiva 12,13 . Logo após o celebre experimento de Miller 2 , diversos pesquisadores colocaram a seguinte questão: os aminoácidos formados na atmosfera, que não fossem destruídos pela forte radiação ultravioleta do nosso jovem Sol, cairiam no mar da Terra primitiva e sendo este mar muito grande (como é nos dias de hoje) os aminoácidos seriam muito diluídos impossibilitando a formação de peptídeos ou proteínas e, desta forma, impedindo a evolução molecular. O mesmo problema ocorreria para o caso dos aminoácidos produzidos em fontes hidrotermais ou no mar ou trazidos por cometas ou meteoros que caíssem no mar. Para resolver o problema da grande diluição dos aminoácidos, Bernal 14 sugeriu que os minerais tivessem um papel importante na pré-concentração dos aminoácidos, devido a suas propriedades de bons adsorventes, e agissem também como catalisadores na formação dos peptídeos e proteínas. Portanto, os minerais poderiam ter selecionado os aminoácidos e catalisado sua reação para formação de peptídeos e proteínas. Neste artigo vamos tratar da questão da participação dos minerais na pré-concentração dos aminoácidos. ADSORÇÃO DE BIOMOLÉCULAS SOBRE MINERAISDevemos salientar que os minerais obviamente tiveram provavelmente também uma participação importante na adsorção de ...

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Reverse micelles as hosts for proteins and small molecules

Cited by 779 publications

References 157 publications

Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles

Synthesis, Functionalization, and Design of Magnetic Nanoparticles for Theranostic Applications

Adsorção de aminoácidos sobre minerais e a origem da vida

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