S–S bonds are not required for the sonochemical formation of proteinaceous microspheres: the case of streptavidin

Avivi, S.; Gedanken, Aharon

doi:10.1042/bj20020676

Cited by 77 publications

(61 citation statements)

References 17 publications

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“…[38] Two proteins were examined, BSA and a-amylase. The surfactants used in these experiments were SDS (sodium dodecyl sulphate), CTAB (cetyltrimethyl ammonium bromide), Oleic acid, Tween 40, and Tween 80.…”

Section: Wwwchemeurjorgmentioning

confidence: 99%

“…[20] Two other investigations probing the biological activity of PMs were conducted in Gedankens group. [23,24] In the first, avidin microspheres were prepared by using the sonochemical method. It was found that these microspheres can bind biotin, but to a lesser degree than the native protein.…”

Section: Are Proteinaceous Microspheres Biologicallymentioning

confidence: 99%

“…In a second study related also to the biological activity of PMs, Avivi [24] formed microspheres of a-amylase (1,4-a-dglucanohydrolase, endoamylase), a protein known to hydrolyze starch, glycogen, and related polysaccharides by randomly cleaving the internal a-1,4-glucosidic linkages. [29] Microspheres of a-amylase were compared for their catalytic activity with those of the native protein.…”

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Preparation and Properties of Proteinaceous Microspheres Made Sonochemically

Gedanken

2008

Chemistry A European J

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In 1990, Suslick and co-workers developed a method in which they used high-intensity ultrasound to make aqueous suspensions of proteinaceous microcapsules filled with water-insoluble liquids, and demonstrated the chemical mechanism of their formation. Suslick's paper opened up a new field that is reviewed in the current manuscript, and this article will attempt to review the experiments that have been conducted since the discovery of this phenomenon. It will answer questions regarding the mechanism of the formation of the microspheres, whether the sonication denaturates the protein or if its biological activity is maintained, and, finally, will address possible applications of the proteinaceous microspheres. Proteinaceous microbubbles will be referred to as proteinaceous microspheres (PM) throughout this review, although they may not have a perfect spherical shape in all cases. This review will start with a short introduction to sonochemistry, although this topic is, and has been reviewed frequently. The review covers literature published until December 2006.

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Section: Wwwchemeurjorgmentioning

confidence: 99%

Section: Are Proteinaceous Microspheres Biologicallymentioning

confidence: 99%

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confidence: 99%

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Preparation and Properties of Proteinaceous Microspheres Made Sonochemically

Gedanken

2008

Chemistry A European J

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“…8 Recently, large poly(R,L-glutamic acid) microspheres (∼5 µm) were reported in passing using ultrasound under strongly acidic conditions. 9 From this prior report, it is probable that their microspheres are not core-shell (n.b., at low pH, PG is insoluble at MW > 6000). Contrary to our results here, Gedanken and coworkers 9 were unable to form microspheres by their methods above pH 4.5.…”

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confidence: 99%

Formation and Characterization of Polyglutamate Core−Shell Microspheres

2006

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The need for organ-targeted delivery of drugs and imaging agents creates an interest in biocompatible, biodegradable vesicles. We make protein microspheres using high-intensity ultrasound; these microspheres have a protein shell and a hydrophobic interior, making them ideal for delivering hydrophobic materials. We have previously shown that various proteins, e.g., bovine serum albumin (BSA), form a microsphere shell stabilized by interprotein cross-linking of cysteine residues. In this study, polyglutamate was used to form core−shell microspheres at slightly basic pH using sonication. These particles are smaller than our previous protein microspheres and are stable under conditions encountered in vivo. The stability of polyglutamate microspheres appears to be due to hydrogen bonding networks and not covalent cross-linking.

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“…For sulfhydryl-free polypeptides (e.g., polyglutamate), hydrogen bonding or ion pairing between carboxylates [13] provided the mechanism for stabilization of oil-filled microparticles. Avivi and Gedanken [14] suggested that hydrophobic interactions in acidic medium are responsible for the fabrication of poly(glutamic acid) and streptavidin microspheres; -SH functional groups are absent in both of these systems.…”

Section: Introductionmentioning

confidence: 99%

Sonochemical synthesis of liquid-encapsulated lysozyme microspheres

Zhou

Leong

Melino

et al. 2010

Ultrasonics Sonochemistry

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a b s t r a c tLiquid-encapsulated lysozyme microspheres were successfully synthesized using a sonochemical method. The encapsulation of four different liquids, namely, sunflower oil, tetradecane, dodecane and perfluorohexane on the formation, stability and morphology of the lysozyme microspheres was studied. Among the four different liquids used for encapsulation, perfluorohexane-filled microspheres were found to be most stable in the dried state with a narrow size distribution. In order to explore the possibility of encapsulating biofunctional molecules (e.g., drugs) within these microspheres, liquids containing a fluorescent dye (Nile red) were encapsulated and the ultrasound-induced release of these dye-loaded liquids was studied. The fluorescence data for the liquid-filled lysozyme microspheres demonstrated the potential use of the sonochemical technique for synthesizing these ''vehicles" for the encapsulation and the controlled delivery of dyes, flavours, fragrances or drugs.

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S–S bonds are not required for the sonochemical formation of proteinaceous microspheres: the case of streptavidin

Cited by 77 publications

References 17 publications

Preparation and Properties of Proteinaceous Microspheres Made Sonochemically

Preparation and Properties of Proteinaceous Microspheres Made Sonochemically

Formation and Characterization of Polyglutamate Core−Shell Microspheres

Sonochemical synthesis of liquid-encapsulated lysozyme microspheres

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