Experimental tensiometric protein adsorption studies

Dunne, Gavin; McMillan, N. D.; O’Rourke, Brian; Morrin, D.; O’Neill, M.; Reidel, S.; McDonell, L.; Scully, Patricia

doi:10.1016/j.colsurfa.2009.06.030

Cited by 4 publications

(2 citation statements)

References 16 publications

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“…This sustained adhesion may be due to the limited and selective protein adsorption mediated by the hydrophilic hydrogel. Extensive studies had shown that protein molecules selectively adsorb onto hydrophobic surfaces via hydrophobic interactions 33 and as a result, the adsorption of adhesion mediating proteins can potentially promote cell adhesion onto more hydrophobic surfaces. Thus, the adhesion results might imply the relative surface hydrophilicity in the following order: TCPS < Photopolymerized PEG hydrogel < PEG SH-Mal hydrogel, which is in good agreement with the contact angle measurement.…”

Section: Resultsmentioning

confidence: 99%

In situ forming poly(ethylene glycol)‐based hydrogels via thiol‐maleimide Michael‐type addition

Kao

2011

J Biomedical Materials Res

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The incorporation of cells and sensitive compounds can be better facilitated without the presence of UV or other energy sources that are common in the formation of biomedical hydrogels such as poly(ethylene glycol) hydrogels. The formation of hydrogels by the step-growth polymerization of maleimide- and thiol-terminated poly(ethylene glycol) macromers via Michael-type addition is described. The effects of macromer concentration, pH, temperature, and the presence of biomolecule gelatin on gel formation were investigated. Reaction kinetics between maleimide and thiol functional groups were found to be rapid. Molecular weight increase over time was characterized via gel permeation chromatography during step-growth polymerization. Swelling and degradation results showed incorporating gelatin enhanced swelling and accelerated degradation. Increasing gelatin content resulted in the decreased storage modulus (G’). The in vitro release kinetics of FITC-labeled dextran from the resulting matrices demonstrated the potential in the development of novel in situ gel-forming drug delivery systems. Moreover, the resulting networks were minimally adhesive to primary human monocytes, fibroblasts and keratinocytes thus providing an ideal platform for further biofunctionalizations to direct specific biological response.

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Section: Resultsmentioning

confidence: 99%

In situ forming poly(ethylene glycol)‐based hydrogels via thiol‐maleimide Michael‐type addition

Kao

2011

J Biomedical Materials Res

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“…Proteins are amphoteric molecules and therefore lower the surface tension of aqueous solutions [33,34]. This property is provided by the building blocks that proteins are made from.…”

Section: Surface Tension Measurementsmentioning

confidence: 99%

Boosting the stability of protein emulsions by the synergistic use of proteins and clays

2012

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The preparation and the properties of high-pressure emulsions based on five different proteins are reported. As proteins, we used the well-studied bovine serum albumin (BSA), a biotechnical produced hydrophobin called H Star Protein B® (HPB), a protein isolate from soybeans, a wheat protein isolate (Plantasol W), and a commercially available yeast extract. All emulsions were characterized by visual appearance, light microscopy, conductivity, and rheological measurements. Beside the emulsion based on soy protein isolate, all other samples showed phase separation under the used conditions (0.5 wt.% protein; 50 wt.% oil). Plantasol W and yeast extract formed the most unstable emulsions showing typical instability processes like coalescence. Gel-like properties have been observed for emulsions based on BSA, soy protein isolate, and HPB. The same proteins were also used to stabilize emulsions after their adsorption on clay particles. Interestingly, all emulsions had gel-like properties with a yield stress value and were stable to the used conditions. It is concluded that the gel character results from the stickiness of the protein covered oil droplets and is independent from the used protein type. The proteins which are adsorbed on the oil droplets can still interact and bind to proteins on other oil droplets.

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New tensiographic approach to surface studies of protein kinetics showing possible structural rearrangement of protein layers on polymer substrates

McMillan¹,

Dunne

Smith

et al. 2010

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Experimental tensiometric protein adsorption studies

Cited by 4 publications

References 16 publications

In situ forming poly(ethylene glycol)‐based hydrogels via thiol‐maleimide Michael‐type addition

In situ forming poly(ethylene glycol)‐based hydrogels via thiol‐maleimide Michael‐type addition

Boosting the stability of protein emulsions by the synergistic use of proteins and clays

New tensiographic approach to surface studies of protein kinetics showing possible structural rearrangement of protein layers on polymer substrates

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