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Adelaide, Australia

Szili E.J.,Flinders University | Szili E.J.,University of South Australia | Kumar S.,University of South Australia | DeNichilo M.,TGR BioSciences | And 2 more authors.
Surface and Coatings Technology | Year: 2010

Osseointegration is a complex process governed by the interaction of many cell types including blood cells (erythrocytes, platelets and leukocytes), phagocytic cells (macrophages) and bone cells (osteoblasts and osteoclasts) on or near the implant surface. The implant surface can be modified through a variety of methods in order to achieve control of some of these cellular interactions and consequently increase the degree of implant fixation with the surrounding bone tissue. In this investigation, titanium was coated with hydroxylated silica by plasma enhanced chemical vapour deposition (PECVD) to increase the surface hydrophilicity and generate reactive surface silanol groups. Subsequently, the silica-coated titanium surface was further modified through silanisation to generate surfaces bearing different reactive chemical functionalities consisting of aldehydes, epoxides and isocyanates, which can react with the amino groups of proteins and growth factors. 2,2,2-trifluoroethylamine (FEAM) was reacted on these surfaces to determine the coupling efficiency of the different surface chemical functionalities. The amino group of FEAM can react with an amino-reactive surface functional group to form a surface terminated with 3 fluorine atoms per FEAM molecule that can be detected by X-ray photoelectron spectroscopy. By analysing the techniques used for protein attachment with the FEAM model molecule, a successful method for isocyanate/amine coupling was found and later adapted for tethering IGF-1 molecules to the functionalised PECVD silica-coated titanium surface. Therefore, this simple method of preliminary testing protein reactivity may prove to be a cost effective strategy in the development of new biomaterial surfaces modified using protein bioconjugation methods. © 2010.


Osmond-McLeod M.J.,CSIRO | Osmond R.I.W.,TGR BioSciences | Oytam Y.,CSIRO | McCall M.J.,CSIRO | And 6 more authors.
Particle and Fibre Toxicology | Year: 2013

Background: Inhaled nanoparticles have been reported in some instances to translocate from the nostril to the olfactory bulb in exposed rats. In close proximity to the olfactory bulb is the olfactory mucosa, within which resides a niche of multipotent cells. Cells isolated from this area may provide a relevant in vitro system to investigate potential effects of workplace exposure to inhaled zinc oxide nanoparticles.Methods: Four types of commercially-available zinc oxide (ZnO) nanoparticles, two coated and two uncoated, were examined for their effects on primary human cells cultured from the olfactory mucosa. Human olfactory neurosphere-derived (hONS) cells from healthy adult donors were analyzed for modulation of cytokine levels, activation of intracellular signalling pathways, changes in gene-expression patterns across the whole genome, and compromised cellular function over a 24 h period following exposure to the nanoparticles suspended in cell culture medium.Results: ZnO nanoparticle toxicity in hONS cells was mediated through a battery of mechanisms largely related to cell stress, inflammatory response and apoptosis, but not activation of mechanisms that repair damaged DNA. Surface coatings on the ZnO nanoparticles mitigated these cellular responses to varying degrees.Conclusions: The results indicate that care should be taken in the workplace to minimize generation of, and exposure to, aerosols of uncoated ZnO nanoparticles, given the adverse responses reported here using multipotent cells derived from the olfactory mucosa. © 2013 Osmond-McLeod et al.; licensee BioMed Central Ltd.


Buckley J.D.,University of South Australia | Thomson R.L.,University of South Australia | Coates A.M.,University of South Australia | Howe P.R.C.,University of South Australia | And 2 more authors.
Journal of Science and Medicine in Sport | Year: 2010

There is evidence that protein hydrolysates can speed tissue repair following damage and may therefore be useful for accelerating recovery from exercise induced muscle damage. The potential for a hydrolysate (WPIHD) of whey protein isolate (WPI) to speed recovery following eccentric exercise was evaluated by assessing effects on recovery of peak isometric torque (PIT). In a double-blind randomised parallel trial, 28 sedentary males had muscle soreness (MS), serum creatine kinase (CK) activity, plasma TNFα, and PIT assessed at baseline and after 100 maximal eccentric contractions (ECC) of their knee extensors. Participants then consumed 250 ml of flavoured water (FW; n = 11), or FW containing 25 g WPI (n = 11) or 25 g WPIHD (n = 6) and the assessments were repeated 1, 2, 6 and 24 h later. PIT decreased ∼23% following ECC, remained suppressed in FW and WPI, but recovered fully in WPIHD by 6 h (P = 0.006, treatment × time interaction). MS increased following ECC (P < 0.001 for time), and remained elevated with no difference between groups (P = 0.61). TNFα and CK did not change (P > 0.45). WPIHD may be a useful supplement for assisting athletes to recover from fatiguing eccentric exercise. © 2008 Sports Medicine Australia.


Trademark
TGR BioSciences | Date: 2012-03-13

Reagent kits comprising antibodies for conducting immunoassays for medical or veterinary diagnostic purposes.


Patent
TGR BioSciences | Date: 2012-03-30

The present disclosure relates to a one-step immunoassay, in which a solid substrate is pre-coated with an immobilisation agent, and whereby the capture agent, the analyte and the detection agent are added to the solid substrate together, followed by a wash step prior to detection. Methods and kits for detecting an analyte in a sample are disclosed. The capture agent can bind the analyte and comprises a ligand for an immobilisation agent. Certain embodiments are directed to antibody capture agents and/or antibody detectable agents. Certain embodiments are directed to a ligand comprising a peptide tag and an immobilisation agent comprising an anti-peptide tag antibody. Certain embodiments are directed to detection of more than one analyte.

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