Residual Byproducts of Peroxide Crosslinked Vitamin E-Blended Ultrahigh Molecular Weight Polyethylene.

BACKGROUND: Wear resistance of ultrahigh molecular weight polyethylene (UHMWPE) is improved via ionizing radiation crosslinking and subsequent high temperature melting for improved toughness. Our group has previously reported that crosslinking can also be achieved chemically using organic peroxides. However, volatile peroxide byproducts are generated during consolidation. The purpose of this study was to quantify elution of volatile peroxide byproducts from UHMWPE before and after in vivo implantation, and to determine their effects on local tissues. METHODS: We prepared crosslinked UHMWPE samples with 5 times the nominal concentration of peroxide needed for improved wear resistance. Control samples (not crosslinked), crosslinked samples, and crosslinked high temperature melting samples were implanted subcutaneously in New Zealand white rabbits for 28 days. Fourier-transform infrared spectroscopy (FTIR) was used to quantify elution of residual peroxide byproducts, and biocompatibility was determined via histological analysis of periprosthetic tissues. RESULTS: Fourier-transform infrared spectroscopy demonstrated elution of residual peroxide byproducts in vivo. No histological differences were observed between tissues in contact with any of the 3 groups of implants; tissues were characterized by fibrosis and a synovial-like lining for all groups. CONCLUSION: UHMWPE chemically crosslinked with very high concentration of organic peroxide did not show any detrimental changes to surrounding subcutaneous tissues, further demonstrating feasibility of crosslinking UHMWPE with a peroxide, rather than irradiation, for the potential use of the material as a bearing surface for joint arthroplasty.

Metal effects on the membrane interactions of amyloid-beta peptides.

A beta (1-42) peptide, found as aggregated species in Alzheimer's disease brain, is linked to the onset of dementia. We detail results of 31P and 2H solid-state NMR studies of model membranes with A beta peptides and the effect of metal ions (Cu2+ and Zn2+), which are found concentrated in amyloid plaques. The effects on the lipid bilayer and the peptide structure are different for membrane incorporated or associated peptides. Copper ions alone destabilise the lipid bilayer and induce formation of smaller vesicles, but not when A beta(1-42) is associated with the bilayer membrane. A beta (25-35), a fragment from the C-terminal end of A beta(1-42), which lacks the metal coordinating sites found in the full length peptide, is neurotoxic to cortical cortex cell cultures. Addition of metal ions has little effect on membrane bilayers with A beta (25-35) peptides. 31P magic angle spinning NMR data show that A beta (1-42) and A beta (1-42)-Cu2+ complexes interact at the surface of anionic phospholipid membranes. Incorporated peptides, however, appear to disrupt the membrane more severely than associated peptides. Solid-state 13C NMR was used to compare structural changes of A beta (1-42) to those of A beta (25-35) in model membrane systems of anionic phospholipids and cholesterol. The A beta peptides appeared to have an increase in beta-strand structure at the C-terminus when added to phospholipid liposomes. The inclusion of Cu2+ also influenced the observed chemical shift of residues from the C-terminal half, providing structural clues for the lipid-associated A beta/metal complex. The results point to the complex pathway(s) for toxicity of the full-length peptide.