FITC BSA

Ioversol 0.1 mmol L FITC-BSA 0.07 mmol L P743 0.1 mmol L P749 0.1 mmol L P840 0.1 mmol L ... 

Our data show that the clearance of the three MIMs tested was lower than that of the nonspecific and highly diffusible agent ioversol (Table 4). The model was validated by the use of FITC-BSA, which had a very low clearance from the upper part of the Transwell filters. 

Figure 14. Typical FRAP data curves obtained with (a) 2 mM SDS in 2 mM sodium phosphate buffer, pH 7.0 containing 0.1 M NaCl and 14 /xM ODAF (b) FITC-BSA (0.5 mg/ml) in distilled water, pH 8.0, at an equilibrium film thickness of 83 nm (c) FITC-BSA (0.2 mg/ml) in 50 mM Na acetate buffer, pH 5.4 at an equilibrium common black film thickness of 14 nm.

The solution diffusion properties of FITC-labelled BSA were measured by FRAP [12], The results showed that the protein diffused freely in solution with a diffusion coefficient of approximately 3xl0 7 cm2/s. This was in reasonable agreement with previously published values [36]. FRAP measurements were also made on thin films stabilized by FITC-BSA. The films were allowed to drain to equilibrium thickness before measurements were initiated. Thin films covering a range of different thicknesses were studied by careful adjustment of solution conditions. BSA stabilized films that had thicknesses up to 40 nm showed no evidence of surface diffusion as there was no return of fluorescence after the bleach pulse in the recovery part of the FRAP curve (Figure 14(c)). In contrast, experiments performed with thin films that were > 80 nm thick showed partial recovery (55%) of the prebleach level of fluorescence (Figure 14(b)). This suggested the presence of two classes of protein in the film one fraction in an environment where it was unable to diffuse laterally, as seen with the films of thicknesses < 45 nm, and a second fraction that was able to diffuse with a calculated diffusion coefficient of lxlO 7 cm2/s. This latter diffusion coefficient was 3 times slower than that... 

There are several recent examples of the switching of nonspecific protein binding on polymer surfaces by application of an external stimulus. Alexander and coworkers demonstrated that protein adhesion can be controlled on PNIPAM surface brushes [14, 181]. For instance, it was reported that the adsorption of FITC-labeled bovine serum albumin (FITC-BSA) on PNIPAM/hexadecanethiol micropatterned surfaces could be tuned by LCST. However, this effect was found to be less pronounced after prolonged incubation times or repeated heating/cooling cycles. The authors suggested that this behavior could be due to unspecific PNIPAM-protein interactions [14],... 

Thermally responsive polymers, such as poly( V-isopropyl acrylamide) (NI-PAm), have also been studied extensively for applications related to those previously discussed [112], De las Heras et al. described the synthesis and patterning of NIPAm brushes on SAMs and their subsequent performance during temperature-dependent adhesion assays of BSA and Streptococcus mutans (Fig. 7). The authors employed p.CP to pattern features of hydrophobic hexadecanethiol and backfilled the surface with an initiator-functionalized alkanethiol. Polymer brushes were grown via surface-initiated atom transfer radical polymerization (ATRP). FITC-BSA was then... 

Fig. 7 (a) Growth of temperature-dependent, patterned polymer brushes on SAMs on gold surfaces. Images show adhesion of (b) FITC-BSA after incubation at 37°C and rinse at 12°C (c) S. mutans after incubation at 4°C for 1 h and (d) S. mutans after incubation at 37°C for 1 h. Reproduced from [112] with permission. Copyright The Royal Society of Chemistry, 2005... 

Ramesh, V. D., Medlicott, N., Razzak, M., and Tucker, I. G. (2002), Microencapsulation of FITC-BSA into poly(e-caprolactone) by a water-in-oil-in-oil solvent evaporation technique. Trends Biomater. Artif. Organs, 15, 31-36. 

Thermogels that take advantage of the hydrolytic properties of polyacetals have also been explored. Schacht et al. have reported the synthesis of graft copolymers comprised of a polyacetal backbone with pendant PEG chains. Incorporation of FITC-BSA at 1 wt.% into the thermogels resulted in a sustained release over about 100 days at pH 7.4 and 40 days at pH 5.5. Release of FITC-BSA occurred by a process that appears to be erosion-controlled [8]. 

E. Schacht, V. Toncheva, K. Vandertaelen, J. Heller, Polyacetal and poly(ortho ester)-poly(ethylene glycol) graft copolymer thermogels preparation, hydrolysis and FITC-BSA release studies, J. Control. Release 116 (2006) 219-225. 

FITC-BSA (Model Immunization Protein), Urease potential study... 

FIGURE 25.7 Fluorescence micrographs of the nasal tissue of rats excised following administration of (A) FITC-BSA solution (B) FITC-BSA encapsulated in plain liposomes or (C) FITC-BSA encapsulated in glycol chitosan coated liposomes. (From Khatri, K. et ah, Vaccine, 26, 2225, 2008. With permission.)... 

Fig. 3 Stability of PLL-coated BSA nanoparticles based on release profile of FITC-BSA from the nanoparticles in phosphate buffer (pH 7.4). PLL of molecular mass 0.9 kDa (a), 4.2 kDa (b), 13.8 kDa (c), and 24 kDa (d) at concentrations of 0.1 mg/mL (filled circles), 0.3 mg/mL (open circles), and 1.0 mg/mL (filled inverted triangles) were used for coating onto BSA nanoparticles [107]...

Figure 10.33. Effect of varying the feed rate of the core stream on the average fiber diameter of the core/shell nanofiber with a fitc-BSA/polycaprolactone core and a PEG shell [131]...

---