title: Comparative analysis of human serum albumin adsorption and complement activation for intraocular lenses.
abstract: Intraocular liquid, in contrast to blood, has no cellular components; therefore, proteins (human serum albumin [HSA], and [alpha, beta, gamma] globulins) are the major components that determine patients' response to the intraocular lens (IOL) surface. In addition to the amount of adsorbed proteins, the possibility of its conformational changes, including conformational changes of globulins C1 and C3 that respond for the activation of the complements system by the classical and alternative pathways, cannot be excluded. The interaction between IOLs and protein components of intraocular liquid directly influences the ocular exudative reaction in the early postoperational period, the intensity of cellular and pigmental scurf on the surface of the IOLs, and the state of endothelial cells of the cornea in the distant postoperational period. Our goal was to compare the interaction of commercial IOLs made from polymethylmethacrylate, silicone, poly-2-hydroxyethyl methacrylate (p-HEMA), and copolymer p-HEMA with collagen with HSA and the complement system. The total internal reflection fluorescence (TIRF) method and hemolytic assay were used for this task, respectively. It has been demonstrated that the probability of biocompatibility of commercially produced IOLs on the stage of protein adsorption can be evaluated using the kinetic of HSA-fluorescein isothiocyanate adsorption onto the IOL surface by the TIRF METHOD: In the case of IOLs from p-HEMA, a negative correlation was shown between the degree of irreversible adsorption of HSA and the minimum relative rate constant of the surface-induced complement activation. We did not find any correlation between hydrophilicity/hydrophobicity of lenses and their adsorptional properties including complement activation. From suggested adsorptional criteria in vitro for biocompatible surfaces, the hydrogel lens from p-HEMA has a lower probability of biocompatibility in comparison with other IOLs.
authors.affiliation: Moscow Institute of Physics and Technology, Moscow, Russia.
authors.forename: E N
authors.initials: EN
authors.lastname: Pokidysheva
authors.forename: I A
authors.initials: IA
authors.lastname: Maklakova
authors.forename: Z M
authors.initials: ZM
authors.lastname: Belomestnaya
authors.forename: N V
authors.initials: NV
authors.lastname: Perova
authors.forename: S N
authors.initials: SN
authors.lastname: Bagrov
authors.forename: V I
authors.initials: VI
authors.lastname: Sevastianov
mesh_terms: D000327:Adsorption; D001672:Biocompatible Materials / Q000737:chemistry; D003094:Collagen / Q000737:chemistry; D003167:Complement Activation; D005453:Fluorescence; D006801:Humans; D020100:Hydrogels / Q000737:chemistry; D007700:Kinetics; D007910:Lenses, Intraocular; D008422:Materials Testing; D008689:Methacrylates / Q000737:chemistry; D019904:Polymethyl Methacrylate / Q000737:chemistry; D012709:Serum Albumin / Q000378:metabolism*; D012828:Silicones / Q000737:chemistry; D013499:Surface Properties
chemical_list: D001672:Biocompatible Materials; D020100:Hydrogels; D008689:Methacrylates; D012709:Serum Albumin; D012828:Silicones; C005044:hydroxyethyl methacrylate; D003094:Collagen; D019904:Polymethyl Methacrylate