Surface characterization, protein adsorption, and initial cell–surface reactions on glutathione and 3‐mercapto‐1,2,‐propanediol immobilized to gold

Abstract

Abstract:Monolayers of glutathione (GSH) and 3-mercapto-1,2-propanediol (MG) on gold were tested for their bioreactivity by assessing the degree of inflammatory reaction as manifested by the adherence and activation of platelets and white blood cells (wbc) after exposure to blood ex vivo. Surface composition was characterized by XPS, and noncontact optical profilometry was used to determine surface roughness. The thickness and composition of the adsorbed protein layers were measured by ellipsometry/ antibody techniques in vitro. Cell adhesion and activation were quantified by acridine orange staining, fluoresceindiacetate staining, and by specific antibodies against cell membrane antigens. Distinct differences among the surfaces were observed relative to the amounts and composition of adsorbed plasma proteins and the adhesion and activation of platelets (CD62P-exposure) and wbc (CD11b/CD18-exposure). GSH surfaces, which adsorbed the least amount of plasma protein, caused the least adherence and activation of platelets (CD62P), followed by the highest activation of wbc (CD11b/18). The MG surfaces caused a rapid recruitment and activation of platelets (CD62P), followed by a lower activation of wbc (CD11b/18). Thus it appears that measurements of the initial adsorption of plasma protein from anticoagulated plasma and of the adhesion and activation of platelets after 8 min of exposure to whole blood cannot be used to predict accurately the adhesion and activation behavior of inflammatory cells after longer periods (2 h) of exposure on different surfaces.

Glutathione adsorption from UHV to the liquid phase at various pH on gold and subsequent modification of protein interaction

“…The second one, at 286.2 ± 0.1 eV, is assigned to carbon in C-N and C-S bonds, the third one at 287.7 ± 0.1 eV to carbon of amide functions and the highest BE peak, at 289.1 ± 0.1 eV to carbon of COOH function of the acidic or carboxylate groups for the basic or zwiterrionic form of GSH. [5,15,16] The N 1s peak presents two contributions for both the acidic and zwiterrionic forms, at 399.7 ± 0.1 and 401.3 ± 0.1 eV respectively, attributed to nitrogen of amide groups and NH 3 + [2,17] ; note that the intensity ratio NH 3 + /O C-NH = 1/2 is in agreement with the molecular formula of GSH. For the anionic form, there is only one contribution at 399.7 ± 0.1 eV assigned to nitrogen in NH 2 and in the amide functions (O C-NH).…”

Adsorption kinetics of l-glutathione on gold and structural changes during self-assembly: an in situATR-IR and QCM study

“…8 GSH-modified gold surfaces were considered for specific protein binding. 9 Furthermore, GSH SAMs on gold electrodes exhibited ''ion gating'' when interacting with rare earth metal ions, transition metal ions, neurotransmitters and a cationic drug. Interaction with these analytes opened up free electrode surface as revealed by redox ion probes.…”

Controlling the morphology of polyurethane/polystyrene interpenetrating polymer networks for enhanced blood compatibility

“…Otherwise, the difference of surface roughness was large enough to affect the conformational change of fibrinogens adsorbed, and adsorption kinetic of fibrinogen. Thus, it became a predominant factor on the adsorption of fibrinogens, and the formation of adsorbed multiplayer of fibrinogens 9–13, 27. SI‐1 had a rougher surface than the other samples, and relatively large amounts of BPFs were adsorbed upon the SI‐1 compared with the other samples.…”

“…Particularly, the surface roughness affects the adsorption of proteins, and platelets. The initial protein adsorption, and cell attachment on a surface is increased, as the surface roughness is increased, and this effect is related to the size of proteins and cells adhered 9–13…”