Tribological performance and tribochemical processes in a DLC/steel system when lubricated in a fully formulated oil and base oil

Diamond-like carbon (DLC) coatings show extremely good promise for a number of applications in automotive components as they exhibit excellent tribological properties such as low friction and good wear resistance. This can impact on improved fuel economy and durability of the engine components. Much work has been reported on the dry sliding of DLC coatings with less so in lubricated contacts and, as such, there is a need to further understand the tribochemistry of lubricated DLC contacts. Commercially-available oils are normally optimised to work on ferrous surfaces. Previous studies on DLC lubricated contacts have tended to use model oil systems rather than fully formulated lubricants and from this an interesting picture of lubrication mechanisms is emerging. Optimising compatibility between a surface and a set of lubricant additives may lead to excellent durability (wear) as well as increased fuel economy (low friction). In this work, the friction and wear properties of a DLC coating under boundary lubrication conditions have been investigated and the tribological performance compared with that of an uncoated steel system. A pin-on-plate tribotester was used to run the experiments using High speed steel (HSS) M2 grade plates coated with 15 at.% hydrogenated DLC (a-C:15H) sliding against cast iron pins. A Group III mineral base oil, fully synthetic Group IV PAO and four different fully formulated oils were used in this study. Furthermore optical and scanning electron microscopes (SEM) were used to observe the wear scar and to assess the durability of the coatings. Energy-Dispersive X-ray analysis (EDX), X-ray Photoelectron Spectroscopy (XPS) and Raman spectroscopy analyses were performed on the tribofilms to understand the tribochemical interactions between oil additives and the a-C:15H coating. This study show that the durability of the a-C:15H coating strongly depends on the selected additive package in the oils. In addition the effect of detergent, dispersant and antioxidants on the performance of the molybdenum-based friction modifier (Mo-FM) and ZDDP anti-wear additive was investigated and results are reported in this paper

Missense Mutations in the N-Terminal Domain of Human Phenylalanine Hydroxylase Interfere with Binding of Regulatory Phenylalanine

Hyperphenylalaninemia due to a deficiency of phenylalanine hydroxylase (PAH) is an autosomal recessive disorder caused by >400 mutations in the PAH gene. Recent work has suggested that the majority of PAH missense mutations impair enzyme activity by causing increased protein instability and aggregation. In this study, we describe an alternative mechanism by which some PAH mutations may render PAH defective. Database searches were used to identify regions in the N-terminal domain of PAH with homology to the regulatory domain of prephenate dehydratase (PDH), the rate-limiting enzyme in the bacterial phenylalanine biosynthesis pathway. Naturally occurring N-terminal PAH mutations are distributed in a nonrandom pattern and cluster within residues 46–48 (GAL) and 65–69 (IESRP), two motifs highly conserved in PDH. To examine whether N-terminal PAH mutations affect the ability of PAH to bind phenylalanine at the regulatory domain, wild-type and five mutant (G46S, A47V, T63P/H64N, I65T, and R68S) forms of the N-terminal domain (residues 2–120) of human PAH were expressed as fusion proteins in Escherichia coli. Binding studies showed that the wild-type form of this domain specifically binds phenylalanine, whereas all mutations abolished or significantly reduced this phenylalanine-binding capacity. Our data suggest that impairment of phenylalanine-mediated activation of PAH may be an important disease-causing mechanism of some N-terminal PAH mutations, which may explain some well-documented genotype-phenotype discrepancies in PAH deficiency