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Källtorp, Mia; Carlén, Anette; Thomsen, Peter; Olsson, J.; Tengvall, Pentti

doi:10.1023/a:1008935826310

Cited by 18 publications

(7 citation statements)

References 46 publications

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“…The PEG constituent does not merely play a role in preventing the particles from being anchored by proteins, but more importantly, it diminishes the opportunity of the nanospheres to attach to the cell membrane which may be induced by various interactions. In contrast, gold possesses a high affinity to biomacromolecules including various immunoglobulins, albumins, and fibrinogen residing in vivo conditions in comparison to a hydroxylated surface . Likewise, the exterior gold layer of Au@ PLLA-PEG@PNIPAAm-PDLA is, at the first stage, supposedly coated with a variety of proteins in the cell media, whereas PLLA-PEG@PNIPAAm-PDLA does not undergo the same binding process.…”

Section: Resultsmentioning

confidence: 99%

Thermosensitive Nanospheres with a Gold Layer Revealed as Low-Cytotoxic Drug Vehicles

Qin

Ihm

et al. 2005

Langmuir

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In this paper, the positive effect of a gold layer on cell viability is demonstrated by examining the results given by 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfop henyl)-2H-tetrazolium (MTS) assay and two-color cell fluorescence viability (TCCV) assay. These cytotoxicity tests were performed with human cervical adenocarcinoma cells (HeLa cell line) and transformed African green monkey kidney fibroblast cells (Cos-7 cell line). To fabricate the nanostructures as drug vehicles, first, poly(l,l-lactide-co-ethylene glycol) (PLLA-PEG) and poly(N-isopropylacrylamide-co-D,D-lactide) (PNIPAAm-PDLA) were synthesized, and then two kinds of thermosensitive nanospheres comprising "shell-in-shell" structures without a gold layer (PLLA-PEG@PNIPAAm-PDLA) and with a gold layer (Au@PLLA-PEG@PNIPAAm-PDLA) were constructed by a modified double-emulsion method (MDEM). Both of them displayed a unique thermosensitive character exhibiting the lower critical solubility temperature (LCST) at 36.7 degrees C which was confirmed by UV-vis spectroscopy and differential scanning calorimetry (DSC). The release profiles of entrapped bovine serum albumin (BSA) were monitored at 22 and 37 degrees C, respectively, to reveal the thermal dependence on the release rate. In cell viability tests, both PLLA-PEG@PNIPAAm-PDLA and Au@PLLA-PEG@PNIPAAm-PDLA showed excellent cell viability, and furthermore, Au@PLLA-PEG@PNIPAAm-PDLA, particularly at high doses, exhibited more enhanced cell viability than PLLA-PEG@PNIPAAm-PDLA. This effect is mainly attributed to the gold layer which binds the protein molecules first and consequently facilitates transmembrane uptake of essential nutrients in the cell media, resulting in favorable cell proliferation.

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Section: Resultsmentioning

confidence: 99%

Thermosensitive Nanospheres with a Gold Layer Revealed as Low-Cytotoxic Drug Vehicles

Qin

Ihm

et al. 2005

Langmuir

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“…Surface energies of protein-adsorbed surfaces were analyzed as discussed in Section . The gel electrophoresis technique has been widely used by various research groups for the quantification of protein desorbed from surfaces using the mechanically assisted SDS elution method. − Briefly, the protein adsorbed on surface-modified coverslips was treated with 3 mL of 5% SDS under the above-stated conditions and later concentrated to 1 mL using Vivaspin 500 centrifugal concentrators (10 kDa cutoff, Sigma, India). The concentrated protein solution (100 μL) was used for electrophoresis analysis using a Mini-PROTEAN System (Bio-Rad Laboratories).…”

Section: Methodsmentioning

confidence: 99%

Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

2018

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Physicochemical interactions of proteins with surfaces mediate the interactions between the implant and the biological system. Surface chemistry of the implant is crucial as it regulates the events at the interface. The objective of this study was to explore the performance of modified surfaces for such interactions relevant to various biomedical applications. Because of a wide range of surface wettability, we aimed to study protein behavior (i.e., conformational changes and their packing) during competitive protein adsorption. Three serum proteins (bovine serum albumin, BSA; fibrinogen, FB; and immunoglobulin G, IgG) were tested for their conformational changes and orientation upon adsorption on hydrophilic (COOH and amine), moderately hydrophobic (mixed and hybrid), and hydrophobic (octyl) surfaces generated via silanization. Modified surfaces were characterized using Fourier-transform infrared spectroscopy, contact angle, and atomic force microscopy (AFM) techniques. Adsorbed masses of proteins from single and binary protein solutions on different surfaces were quantified along with their secondary structure analyses. Maximum adsorbed protein masses were found to be on negatively charged and hydrophobic (octyl) surfaces because of ionic and hydrophobic interactions between protein molecules and surfaces, respectively. Side-on and end-on orientations of adsorbed protein molecules were analyzed using theoretical and AFM analyses. We observed compact and elongated forms of BSA molecules on hydrophilic and hydrophobic surfaces, respectively. We further found a linear increase in the α-helix content of BSA and β-sheet contents of FB and IgG proteins with the increasing side-on (%)-oriented protein molecules on the surfaces. This indicates that side-on orientations of adsorbed FB and IgG lead to the formation of β-sheets. Sodium dodecyl sulfate polyacrylamide gel electrophoresis was employed to quantify the protein types and their ratio in competitively adsorbed proteins on different surfaces. A theoretical analysis was also used to determine the % secondary structures of competitively adsorbed proteins from BSA/FB and BSA/IgG solutions, which very well agreed with experimental results. The competitive protein adsorption from both BSA/FB and BSA/IgG solutions was found to be entropy-driven, as revealed by thermodynamic studies performed using isothermal titration calorimetry.

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“…, methyl, hydroxyl or carboxyl groups) are also being tried to modulate the hydrophilicity of the titanium surface [51]. Peptide sequences have been used as monolayer modifications and shown to promote cell adhesion [52].…”

Section: Titanium Surface Activationmentioning

confidence: 99%

Titanium as a Reconstruction and Implant Material in Dentistry: Advantages and Pitfalls

2012

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Commercial pure titanium (cpTi) has been the material of choice in several disciplines of dentistry due to its biocompatibility, resistance to corrosion and mechanical properties. Despite a number of favorable characteristics, cpTi as a reconstruction and oral implant material has several shortcomings. This paper highlights current knowledge on material properties, passive oxidation film formation, corrosion, surface activation, cell interactions, biofilm development, allergy, casting and machining properties of cpTi for better understanding and potential improvement of this material for its clinical applications.

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Untitled

Cited by 18 publications

References 46 publications

Thermosensitive Nanospheres with a Gold Layer Revealed as Low-Cytotoxic Drug Vehicles

Thermosensitive Nanospheres with a Gold Layer Revealed as Low-Cytotoxic Drug Vehicles

Conformational and Organizational Insights into Serum Proteins during Competitive Adsorption on Self-Assembled Monolayers

Titanium as a Reconstruction and Implant Material in Dentistry: Advantages and Pitfalls

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