Synthesis of nanoparticles with frog foam nest proteins

Choi, Hyo-Jick; Ebersbacher, Charles; Myung, Nosang V.; Montemagno, Carlo

doi:10.1007/s11051-012-1092-1

Cited by 6 publications

(6 citation statements)

References 27 publications

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“…Emulsion/foam stabilisers in food HFBII (hydrophobin) [17,18] Globulin [19] Casein [20] Drug delivery HFBI (hydrophobin) [21] Casein [22] Nanoparticle synthesis Rsn-2 [23] Biomineralization H* Protein B (hydrophobin) [24] Surfactin [25] Remediation Surfactin [26] Exfoliation of 2D materials HFBI (hydrophobin) [27] Vmh2 (hydrophobin) [28] Understanding the biological functions and technological applications of biosurfactant proteins requires knowledge of their structure and behaviour at interfaces. As changes in these environments can occur over nanometre lengthscales, understanding this requires microscopic detail that is challenging to obtain experimentally.…”

Section: Application Protein(s) Referencesmentioning

confidence: 99%

Molecular Dynamics Simulation of Protein Biosurfactants

Cheung

Samantray

2018

Colloids and Interfaces

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Surfaces and interfaces are ubiquitous in nature and are involved in many biological processes. Due to this, natural organisms have evolved a number of methods to control interfacial and surface properties. Many of these methods involve the use of specialised protein biosurfactants, which due to the competing demands of high surface activity, biocompatibility, and low solution aggregation may take structures that differ from the traditional head–tail structure of small molecule surfactants. As well as their biological functions, these proteins have also attracted interest for industrial applications, in areas including food technology, surface modification, and drug delivery. To understand the biological functions and technological applications of protein biosurfactants, it is necessary to have a molecular level description of their behaviour, in particular at surfaces and interfaces, for which molecular simulation is well suited to investigate. In this review, we will give an overview of simulation studies of a number of examples of protein biosurfactants (hydrophobins, surfactin, and ranaspumin). We will also outline some of the key challenges and future directions for molecular simulation in the investigation of protein biosurfactants and how this can help guide future developments.

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Section: Application Protein(s) Referencesmentioning

confidence: 99%

Molecular Dynamics Simulation of Protein Biosurfactants

Cheung

Samantray

2018

Colloids and Interfaces

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“…Histidine-tagged RSN-2 proteins were expressed in E. coli and purified following protocols described previously [18]. The proteins were washed with DI water in a Centricon filtration unit (10 kDa cut-off; Millipore, Billerica, MA).…”

Section: Rsn-2 Preparationmentioning

confidence: 99%

“…The purified protein sample from the eluate of nickelnitrilotriacetic acid resin was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as described previously [18]. Isoelectric point (IEP) was measured with isoelectric focusing (IEF) gel electrophoresis on Novex pH 3-10 IEF gel (Thermo Fisher Scientific, Waltham, MA) following the manufacturer's protocol.…”

Section: Sodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis An...mentioning

confidence: 99%

pH stability and comparative evaluation of ranaspumin-2 foam for application in biochemical reactors

Choi¹,

Ebersbacher²,

Quan³

et al. 2013

Nanotechnology

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Aqueous channels of foam represent a simplified, natural bioreactor on the micro-/nano-scale. Previous studies have demonstrated the feasibility and potential application of foams in replicating cellular process in vitro, but no research has been performed to establish a basis for designing stable and biocompatible foam formulations. Our research has been directed specifically to the evaluation of ranaspumin-2 (RSN-2), a frog foam nest protein. The strong surfactant activity of RSN-2 enabled us to produce foams using low protein concentration (1 mg ml(-1)) over a wide pH range (pH ≥ 3). Importantly, the RSN-2 formulation exhibited the best foam stability at a near neutral pH condition, which shows a potential for application to various biosynthesis applications. Model cellular systems such as liposomes and inactivated A/PR/8/34 influenza virus maintained their physicochemical stability and full hemagglutination activity, indicating biocompatibility of RSN-2 with both cellular membranes and proteins both in bulk solution and in foam. Moreover, the addition of RSN-2 did not exert any deteriorative effects on bacterial cell growth kinetics. In contrast, Tween 20, Triton X-100, and BSA did not show satisfactory performance in terms of foamability, foam stability, physicochemcial stability, and biochemical stability. Although our study has been limited to representative formulations composed of only surfactant molecules, a number of unique advantages make RSN-2 a promising candidate for in vitro foam biosynthesis.

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“…The RSN-2 protein appears to form a clamshell-like structure, which can undergo an unfolding conformational change to expose non-polar patches on the protein surface to the air, while highly polar regions remain in contact with the water interface to provide the surfactant activity. RSN-2 has been successfully used in industry as a surfactant in nanoparticle production [ 20 ], but there could be great potential for the whole nest foam protein composition to be used in a range of pharmaceutical applications.…”

Section: Introductionmentioning

confidence: 99%

Frog nest foams exhibit pharmaceutical foam-like properties

et al. 2021

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Foams have frequently been used as systems for the delivery of cosmetic and therapeutic molecules; however, there is high variability in the foamability and long-term stability of synthetic foams. The development of pharmaceutical foams that exhibit desirable foaming properties, delivering appropriate amounts of the active pharmaceutical ingredient (API) and that have excellent biocompatibility is of great interest. The production of stable foams is rare in the natural world; however, certain species of frogs have adopted foam production as a means of providing a protective environment for their eggs and larvae from predators and parasites, to prevent desiccation, to control gaseous exchange, to buffer temperature extremes, and to reduce UV damage. These foams show great stability (up to 10 days in tropical environments) and are highly biocompatible due to the sensitive nature of amphibian skin. This work demonstrates for the first time that nests of the túngara frog ( Engystomops pustulosus ) are stable ex situ with useful physiochemical and biocompatible properties and are capable of encapsulating a range of compounds, including antibiotics. These protein foam mixtures share some properties with pharmaceutical foams and may find utility in a range of pharmaceutical applications such as topical drug delivery systems.

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Synthesis of nanoparticles with frog foam nest proteins

Cited by 6 publications

References 27 publications

Molecular Dynamics Simulation of Protein Biosurfactants

Molecular Dynamics Simulation of Protein Biosurfactants

pH stability and comparative evaluation of ranaspumin-2 foam for application in biochemical reactors

Frog nest foams exhibit pharmaceutical foam-like properties

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