Adsorption of Modified HIV-1 Capsid p24 Protein onto Thermosensitive and Cationic Core−Shell Poly(styrene)−Poly(<i>N</i>-isopropylacrylamide) Particles

Duracher, David; Elaı̈ssari, Abdelhamid; Mallet, and François; Pichot, Christian

doi:10.1021/la0004045

Cited by 86 publications

(70 citation statements)

References 26 publications

(44 reference statements)

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“…[191] As predicted by numerous studies, at T > VPTT of pNIPAm a higher adsorption was observed which was due to hydrophobic interactions. Similarly Urakami et al studied the phagocytosis of polystyrene-co-polyacrylamide gel particles as a function of hydrophobicity.…”

Section: Biomaterialsmentioning

confidence: 63%

Soft Nanotechnology with Soft Nanoparticles

2005

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The last decade of research in the physical sciences has seen a dramatic increase in the study of nanoscale materials. Today, "nanoscience" has emerged as a multidisciplinary effort, wherein obtaining a fundamental understanding of the optical, electrical, magnetic, and mechanical properties of nanostructures promises to deliver the next generation of functional materials for a wide range of applications. While this range of efforts is extremely broad, much of the work has focused on "hard" materials, such as Buckyballs, carbon nanotubes, metals, semiconductors, and organic or inorganic dielectrics. Meanwhile, the soft materials of current interest typically include conducting or emissive polymers for "plastic electronics" applications. Despite the continued interest in these established areas of nanoscience, new classes of soft nanomaterials are being developed from more traditional polymeric constructs. Specifically, nanostructured hydrogels are emerging as a promising group of materials for multiple biotechnology applications as the need for advanced materials in the post-genomic era grows. This review will present some of the recent advances in the marriage between water-swellable networks and nanoscience.

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Section: Biomaterialsmentioning

confidence: 63%

Soft Nanotechnology with Soft Nanoparticles

2005

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“…[40][41][42][43] Thus it is expected as ppNIPAM surface wettability drops above the LCST, the apparent affinity of soluble protein with the surface increases. 44 Also of note, we find that although the ⌫ max values on PET and ppNIPAM are relatively similar for BSA and antiferritin antibody isotherms, those for fibrinogen adsorption vary with respect to surface and temperature. At 37°C, the ⌫ max values for fibrinogen on both PET and ppNIPAM surfaces are about 550 ng/ cm 2 .…”

Section: A Protein Adsorptionmentioning

confidence: 69%

Temperature dependent activity and structure of adsorbed proteins on plasma polymerized N-isopropyl acrylamide

et al. 2006

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Thorough studies of protein interactions with stimulus responsive polymers are necessary to provide a better understanding of their applications in biosensors and biomaterials. In this study, protein behavior on a thermoresponsive polymer surface, plasma polymerized N-isopropyl acrylamide (ppNIPAM), is investigated using multiple characterization techniques above and below its lower critical solution temperature (LCST). Protein adsorption and binding affinity are probed using radiolabeled proteins. Protein activity is estimated by measuring the immunological activity of an antibody adsorbed onto ppNIPAM using surface plasmon resonance. Conformation/orientation of the proteins is probed by time-of-flight secondary ion mass spectrometry (TOF-SIMS) and principal component analysis (PCA) of the TOF-SIMS data. In this work, we find that at low protein solution concentrations, ppNIPAM-treated surfaces are low fouling below the LCST, but protein retentive above it. The protein adsorption isotherms demonstrate that apparent affinity between soluble protein molecules and the ppNIPAM surface are an order of magnitude lower at room temperature than at 37 °C. Although direct protein desorption is not observed in our study when the surface temperature drops below the LCST, the binding affinity of surface adsorbed protein with ppNIPAM is reduced, as judged by a detergent elution test. Furthermore, we demonstrated that proteins adsorbed onto ppNIPAM are functionally active, but the activity is better preserved at room temperature than 37 °C. The temperature dependent difference in protein activity as well as TOF-SIMS and PCA study suggest that proteins take different conformations/orientations after adsorption on ppNIPAM above and below the LCST.

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“…[14] Therefore, immobilization research has largely focused on matrix selection and on optimizing immobilization conditions. [15][16][17][18] For example, work has addressed support surface hydrophobicity/hydrophobocity [19,20,21] and 3 enzyme solution pH. [17,22,23] These parameters have large influence on the total amount of enzyme loading and enzyme-catalyst activity.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Candida antarctica lipase B on Polystyrene Nanoparticles

Miletić

Abetz²,

Ebert³

et al. 2009

Macromol. Rapid Commun.

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Summary/AbstractPolystyrene (PS) nanoparticles were prepared via a nanoprecipitation process. The influence of the pH of the buffer solution used during the immobilization process on the loading of Candida antarctica lipase B (Cal-B) and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized Cal-B was studied. The pH of the buffer solution has no influence on enzyme loading, while immobilized enzyme activity is very dependent on the pH of adsorption. Cal-B immobilized on polystyrene nanoparticles in buffer solution pH 6.8 performed higher hydrolytic activity than crude enzyme powder and Novozyme 435.

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Adsorption of Modified HIV-1 Capsid p24 Protein onto Thermosensitive and Cationic Core−Shell Poly(styrene)−Poly(N-isopropylacrylamide) Particles

Cited by 86 publications

References 26 publications

Soft Nanotechnology with Soft Nanoparticles

Soft Nanotechnology with Soft Nanoparticles

Temperature dependent activity and structure of adsorbed proteins on plasma polymerized N-isopropyl acrylamide

Immobilization of Candida antarctica lipase B on Polystyrene Nanoparticles

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