Garrett Q, Laycock B, Garrett R W
Cooperative Research Centre for Eye Research and Technology, The University of New South Wales, Sydney, Australia.
Invest Ophthalmol Vis Sci. 2000 Jun;41(7):1687-95.
To examine the effect of hydrogel lens monomer constituents on protein sorption.
A series of hydroxyethylmethacrylate (HEMA)-based hydrogels with various amounts of methacrylic acid (MAA) or N-vinyl pyrrolidone (NVP) were synthesized. A radiolabel tracer technique was used to measure the amount of protein adsorbed on or penetrating into the hydrogels. Penetration of fluorescence-labeled proteins in the hydrogels was studied by laser scanning confocal microscopy. Single-protein solutions of human serum albumin (HSA) and hen egg lysozyme were studied.
Inclusion of the comonomers MAA or NVP in hydrogels resulted in an increase in water content and also had a strong impact on protein sorption. An increase in the amount of MAA in the poly(HEMA-co-MAA) hydrogels increased lysozyme adsorption and penetration but reduced HSA adsorption. However, the amount of protein adsorbed for both HSA and lysozyme increased with the amount of NVP in the poly(HEMA-co-NVP) hydrogels. In contrast to the marked effect of MAA on protein sorption, in particular, on lysozyme sorption, NVP had little influence on protein sorption. When a hydrogel contains both MAA and NVP, MAA has the dominant effect on protein sorption-in particular, on lysozyme sorption. Furthermore, a large difference was observed in the amount of lysozyme adsorbed on the hydrogels that had similar water contents but little variation in adsorption of HSA.
Negatively charged carboxyl groups of the MAA constituent may influence lysozyme sorption in two ways: by electrostatic attraction and by increasing the possibility for the small lysozyme molecule to penetrate the hydrogels. Interactions of the surface lactam groups of NVP with proteins may be attributable to the attraction of proteins to NVP. Water content is not a primary factor in determining protein adsorption. It appears that the monomer constituents, such as MAA or NVP, control protein adsorption.
研究水凝胶镜片单体成分对蛋白质吸附的影响。
合成了一系列含有不同量甲基丙烯酸（MAA）或N-乙烯基吡咯烷酮（NVP）的甲基丙烯酸羟乙酯（HEMA）基水凝胶。采用放射性标记示踪技术测量吸附在水凝胶上或渗透入水凝胶中的蛋白质数量。通过激光扫描共聚焦显微镜研究荧光标记蛋白质在水凝胶中的渗透情况。研究了人血清白蛋白（HSA）和鸡蛋清溶菌酶的单蛋白溶液。
在水凝胶中加入共聚单体MAA或NVP会导致含水量增加，并且对蛋白质吸附也有强烈影响。聚（HEMA-co-MAA）水凝胶中MAA含量的增加会增加溶菌酶的吸附和渗透，但会降低HSA的吸附。然而，聚（HEMA-co-NVP）水凝胶中HSA和溶菌酶的吸附蛋白量均随NVP含量的增加而增加。与MAA对蛋白质吸附，特别是对溶菌酶吸附的显著影响相反，NVP对蛋白质吸附影响很小。当水凝胶同时含有MAA和NVP时，MAA对蛋白质吸附，特别是对溶菌酶吸附起主导作用。此外，在含水量相似的水凝胶上观察到溶菌酶吸附量存在很大差异，但HSA的吸附变化很小。
MAA成分带负电荷的羧基可能通过两种方式影响溶菌酶吸附：通过静电吸引以及增加小分子溶菌酶分子渗透入水凝胶的可能性。NVP的表面内酰胺基团与蛋白质的相互作用可能归因于蛋白质对NVP的吸引力。含水量不是决定蛋白质吸附的主要因素。似乎单体成分，如MAA或NVP，控制着蛋白质吸附。
