Large scale landfarming experiments, using an extensive range of treatments, were conducted in the Niger-Delta, Nigeria to study the degradation of oil in contaminated soils. In this work the effect of nutrient addition, biosurfactant, Eisenia fetida (earthworm) enzyme extract, bulking and sorption agents and soil neutralization were tested. It was found that these treatments were successful in removing up to 53% of the total petroleum hydrocarbon in the soil within 16 weeks. A comparison between treatments demonstrated that most were no more effective than agricultural fertilizer addition alone. One strategy that did show better performance was a combination of nutrients, biochar and biosurfactant, which was found to remove 23% more Total Petroleum Hydrocarbons (TPH) than fertilizer alone. However, when performance normalized costs were considered, this treatment became less attractive as a remedial option. Based on this same analysis it was concluded that fertilizer only was the most cost effective treatment. As a consequence, it is recommended that fertilizer is used to enhance the landfarming of hydrocarbon contaminated soils in the Niger Delta. The attenuation rates of both bulk TPH and Total Petroleum Hydrocarbon Criteria Working Group (TPHCWG) fractions are also provided. These values represent one of the first large scale and scientifically tested datasets for treatment of contaminated soil in the Niger Delta region. An inverse correlation between attenuation rates and hydrocarbon molecular weight was observed with heavy fractions showing much slower degradation rates than lighter fractions. Despite this difference, the bioremediation process resulted in significant removal of all TPH compounds independent of carbon number.

Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer's and Parkinson's disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using a combination of theory, in vitro experiments, simulations of a coarse-grained protein model and meta-data analysis, we delineate the enthalpic and entropic contributions that dominate amyloid fibril elongation. Our prediction of a characteristic temperature-dependent enthalpic signature is confirmed by the performed calorimetric experiments and a meta-analysis over published data. From these results we are able to define the necessary conditions to observe cold denaturation of amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.

Proteins tend to bury hydrophobic residues inside their core during the folding process to provide stability to the protein structure and to prevent aggregation. Nevertheless, proteins do expose some ‘sticky’ hydrophobic residues to the solvent. These residues can play an important functional role, for example in protein-protein and membrane interactions. Here, we investigate how hydrophobic protein surfaces are by providing three measures for surface hydrophobicity: the total hydrophobic surface area, the relative hydrophobic surface area, and - using our MolPatch method - the largest hydrophobic patch. Secondly, we analyse how difficult it is to predict these measures from sequence: by adapting solvent accessibility predictions from NetSurfP2.0, we obtain well-performing prediction methods for the THSA and RHSA, while predicting LHP is more difficult. Finally, we analyse implications of exposed hydrophobic surfaces: we show that hydrophobic proteins typically have low expression, suggesting cells avoid an overabundance of sticky proteins. Availability https://github.com/ibivu/hydrophobic_patches

Background Frontotemporal lobar degeneration (FTLD) is characterized pathologically by neuronal and glial inclusions of hyperphosphorylated tau or by neuronal cytoplasmic inclusions of TDP43. This study aimed at deciphering the molecular mechanisms leading to these distinct pathological subtypes. Methods To this end, we performed an unbiased mass spectrometry-based proteomic and systems-level analysis of the middle frontal gyrus cortices of FTLD-tau (n = 6), FTLD-TDP (n = 15), and control patients (n = 5). We validated these results in an independent patient cohort (total n = 24). Results The middle frontal gyrus cortex proteome was most significantly altered in FTLD-tau compared to controls (294 differentially expressed proteins at FDR = 0.05). The proteomic modifications in FTLD-TDP were more heterogeneous (49 differentially expressed proteins at FDR = 0.1). Weighted co-expression network analysis revealed 17 modules of co-regulated proteins, 13 of which were dysregulated in FTLD-tau. These modules included proteins associated with oxidative phosphorylation, scavenger mechanisms, chromatin regulation, and clathrin-mediated transport in both the frontal and temporal cortex of FTLD-tau. The most strongly dysregulated subnetworks identified cyclin-dependent kinase 5 (CDK5) and polypyrimidine tract-binding protein 1 (PTBP1) as key players in the disease process. Dysregulation of 9 of these modules was confirmed in independent validation data sets of FLTD-tau and control temporal and frontal cortex (total n = 24). Dysregulated modules were primarily associated with changes in astrocyte and endothelial cell protein abundance levels, indicating pathological changes in FTD are not limited to neurons. Conclusions Using this innovative workflow and zooming in on the most strongly dysregulated proteins of the identified modules, we were able to identify disease-associated mechanisms in FTLD-tau with high potential as biomarkers and/or therapeutic targets.

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