Albumin and fibrinogen adsorption onto phosphatidylcholine monolayers investigated by Fourier transform infrared spectroscopy

In vivo biocompatibility and stability of a substrate-supported polymerizable membrane-mimetic film

“…Stability and biocompatibility of the membrane-mimetic coating was demonstrated visually over a 4-week period after implantation of empty modified membrane-mimetic microcapsules in the peritoneal cavity of C57BL/6 mice. Prior studies have suggested that PC-based polymers should be associated with limited cell and protein reactivity, and studies from our group and others have demonstrated that membrane-mimetic surfaces exhibit little protein adsorption or cell adhesion [4][5][6][7][8][9][10]16,17]. However, the biocompatibility of membrane-mimetic films assembled on alginate microcapsules was dependent on the underlying PEM on which the film was assembled, as modified membrane-mimetic capsules were significantly more biocompatible than those originally fabricated.…”

“…Such films have emerged as powerful models of cell and tissue surfaces [2], and have garnered considerable interest as coatings for biosensing devices [3]. Significantly, supported phosphatidylcholine (PC) films have been shown to limit protein adsorption and subsequent cell adhesion in vitro [4][5][6][7][8][9][10], a phenomenon linked to the zwiterionic nature of the PC head group [5]. Despite these favorable characteristics, the use of membrane-mimetic thin films as coatings for implantable biomaterials remains limited, in part, by a lack of stability for most applications outside of a laboratory environment [11,12].…”

Negative regulation of fibrin polymerization and clot formation by nanoparticles of silver

“…5). In general, bands between 1618-1625 cm −1 , 1630-1640 cm −1 , 1645-1655 cm −1 , 1660-1670 cm −1 and 1680-1685 cm −1 are related to ␤ sheet intermolecular (aggregates), ␤ sheet native, ␣ helix, ␤ turns and antiparallel ␤ sheets conformation, respectively [29,30]. Deconvolution of nanosilver-treated fibrinogen amide I band showed significant differences as revealed in Fig.…”

Competitive adsorption of fibrinogen and dipalmitoylphosphatidylcholine at the air/aqueous interface

“…In this article, four types of experiments or protocols are designed to study the competitive adsorption of FB and DPPC at the air/aqueous interface: (i) adsorption of FB/DPPC mixtures from the bulk; (ii) forming an insoluble DPPC spread monolayer via an organic solvent; such a monolayer with a hydrophilic lecithin polar group "facing" the aqueous subphase is a good biomimetic surface which may prevent protein adsorption [24,25]; (iii) introducing a thin aqueous layer of a DPPC dispersion onto the surface of aqueous FB/DPPC with the Trurnit method [26]; the aqueous layer contains no protein and is expected to be inhibited less by the protein in the underlying liquid; the surface of the aqueous FB/DPPC mixture may show similar behavior as in the in vivo aqueous interface of ARDS-damaged lung alveoli, which may also contain other lipids and proteins; (iv) spraying aerosolized DPPC dispersion droplets on the surface of aqueous FB/DPPC to create a thin aqueous layer as in experiment (iii); the DPPC droplets may reach the aqueous surface and adsorb with less interference by the FB; this method would resemble or simulate an aerosol delivery of lung surfactant replacement formulations. In these four protocols, tensiometry, at constant or pulsating area conditions, and direct probing of the surface layers by infrared reflection absorption spectroscopy (IRRAS) and ellipsometry are used to determine the composition and concentration of lipids and proteins at the surface layer.…”