Adsorption of low density lipoproteins onto selected biomedical polymers.
This study examines the interaction of human low density lipoprotein (LDL) with a select group of biomedical polymers. The adsorption characteristics of LDL on cured filler-free poly(dimethyl Siloxane) (C-PDMS), Biomer, Cardiomat 610, Kraton 1650, poly(hydroxyethyl methacrylate) (PHEMA) and glass are presented. Adsorption of LDL to charged hydrophilic glass control surfaces occurred rapidly, reaching plateau concentrations within one minute (0.19 +/- 0.01 ug/cm2). Adsorption of LDL to polymer surfaces appeared to be dependent upon both the polymer hydrophobicity (or apolar nature), and flexibility (or dynamic nature) at the interface. Increased surface concentrations were observed for Biomer (0.32 +/- 0.01 ug/cm2) as well as other polymers which exhibited both hydrophobic and elastomeric properties. Temperature changes between 25 degrees C and 37 degrees C were found to significantly influence the surface concentration of LDL on Biomer (0.16 +/- 0.01 ug/cm2 at 25 degrees C versus 0.32 +/- 0.01 ug/cm2 at 37 degrees C). A lipid core phase transition at 36 degrees C was believed to be responsible for the temperature influence. Preliminary competitive adsorption studies of LDL with albumin (HSA) and serum on silicone surfaces suggests that LDL adsorption occurred rapidly and preferentially (0.25 +/- 0.01 ug/cm2 for LDL alone; 0.33 +/- 0.01 ug/cm2 for LDL + HSA; 0.15 +/- 0.01 ug/cm2 LDL + serum). Preliminary studies on the role of LDL in calcification were not conclusive. It can be concluded that LDL adsorption is dependent upon polymer hydrophobicity, flexibility and temperature. Competitive adsorption experiments suggests that LDL may have a substantial influence on protein adsorption.
D000327:Adsorption; D001672:Biocompatible Materials; D007700:Kinetics; D008077:Lipoproteins, LDL; D011108:Polymers; D012709:Serum Albumin; D013696:Temperature
D001672:Biocompatible Materials; D008077:Lipoproteins, LDL; D011108:Polymers; D012709:Serum Albumin