English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

Dynamic contact angle (DCA) analysis was used to investigate the kinetics and dynamics of proteininteractions in a time-dependent manner for a group of organic natural-based surfaces during theirinitial contact with aqueous and protein solutions. Starch-based biomaterials were used to analyze theinfluence different materials with different surfaces had on the adsorption, desorption andconfiguration of proteins. Polymeric blends of starch and cellulose acetate (SCA), polycaprolactone(SPCL) and ethylene vinyl alcohol (SEVA-C) were used. The model protein systems included singleprotein solutions of human serum albumin, fibronectin, vitronectin and fibrinogen, and also complexsolutions of human blood plasma. In the adsorption studies, very small and nearly equal advancing andreceding contact angles were measured for all the materials. Highly wetting and low contact anglehysteresis, therefore, are exhibited by these surfaces. This effect was more noticeable for SCA surfaces.Moreover, the effect of protein concentration was also assessed and demonstrated to substantiallyaffect the DCA wetting forces of SEVA-C and SPCL surfaces. In the desorption studies, during therinsing phase with saline solution, the DCA loops became larger than that observed for the adsorptionphase, which indicated increases in the contact angle hysteresis. The hysteresis of SCA and SPCLsurfaces reversibly changed through the desorption phase, at the end of which, hysteresis wascomparable to that of surfaces immersed in saline solution. The results indicated that adsorbed proteinscould desorb more readily on SCA and SPCL than on SEVA-C. In the later case, stronger interactionssuch as hydrophobic forces were established and it is likely the rearrangement of protein conformationhad occurred. Monitored by DCA, the evolution of hysteresis demonstrated the progressive bondstrengthening between protein molecules and solid substratum, further elucidating the behaviour ofproteins that regulate cellular interactions with implanted devices.The authors acknowledge funding from the Foundation for Science and Technology (FCT), Portugal for SFRH/BD/11188/2002 and for partial funding through FEDER and POCTI programmes and EU funded Project HIPPOCRATES (NMP3-CT-2003-505758). This work was carried out under the scope of the European Network of Excellence EXPERTISSUES (NMP3-CT-2004-500283)

The dynamics, kinetics and reversibility of protein adsorption onto the surface of biodegradable materials