Accuracy Analysis of a Dam Model from Drone Surveys.

This paper investigates the accuracy of models obtained by drone surveys. To this end, this work analyzes how the placement of ground control points (GCPs) used to georeference the dense point cloud of a dam affects the resulting three-dimensional (3D) model. Images of a double arch masonry dam upstream face are acquired from drone survey and used to build the 3D model of the dam for vulnerability analysis purposes. However, there still remained the issue of understanding the real impact of a correct GCPs location choice to properly georeference the images and thus, the model. To this end, a high number of GCPs configurations were investigated, building a series of dense point clouds. The accuracy of these resulting dense clouds was estimated comparing the coordinates of check points extracted from the model and their true coordinates measured via traditional topography. The paper aims at providing information about the optimal choice of GCPs placement not only for dams but also for all surveys of high-rise structures. The knowledge a priori of the effect of the GCPs number and location on the model accuracy can increase survey reliability and accuracy and speed up the survey set-up operations.

Inflammatory profile in subcutaneous and epicardial adipose tissue in men with and without diabetes.

In recent years, evidence has emerged indicating that insulin resistance and diabetes mellitus type 2 are associated with inflammation of adipose tissue (AT). Interest has been focused on epicardial AT (EAT) because of its possible involvement with atherosclerosis and cardiovascular diseases. The aim of this study was to characterize adipocyte size and inflammatory profile in subcutaneous (SAT) and EAT among subjects with or without diabetes. Biopsies were collected from SAT and EAT in 34 men undergoing elective cardiac surgery. Weight, height, body mass index, waist circumference, as well as serum levels of glucose, insulin, lipids, adiponectin, and leptin were determined in all subjects. Adiponectin, MCP-1, and CD68 mRNA levels present within cells from AT biopsies were determined by real-time polymerase chain reaction. Adipocyte size was determined by optic microscopy and morphometry. Regarding the experimental group as a whole, gene-expression levels within EAT were significantly lower for adiponectin and higher, albeit not significantly, for MCP-1, when compared with that of SAT. In addition, adipocytes in EAT were significantly smaller than those in SAT. Subjects with diabetes showed lower adiponectin gene-expression levels in both SAT and EAT when compared with subjects without diabetes. By contrast, MCP-1 and CD68 gene-expression levels were higher in both tissue types of diabetic subjects. Adipocyte size in EAT was significantly larger in diabetic subjects than in nondiabetic subjects. Our data revealed a predominantly inflammatory profile in both SAT and EAT in subjects with diabetes in comparison with those without diabetes.

Amyloidogenic and non-amyloidogenic molten globule conformation of ß-lactoglobulin in self-crowded regime.

Molecular insights on the ß-lactoglobulin thermal unfolding and aggregation are derived from FTIR and UV Resonance Raman (UVRR) investigations. We propose an in situ and in real-time approach that thanks to the identification of specific spectroscopic markers can distinguish the two different unfolding pathways pursued by ß-lactoglobulin during the conformational transition from the folded to the molten globule state, as triggered by the pH conditions. For both the investigated pH values (1.4 and 7.5) the greatest conformational variation of ß-lactoglobulin occurs at 80 °C and a high degree of structural reversibility after cooling is observed. In acidic condition ß-lactoglobulin exposes to the solvent its hydrophobic moieties in a much higher extent than in neutral solution, resulting on a highly open conformation. Moving from the diluted to the self-crowded regime, the solution pH and consequently the different molten globule conformation select the amyloid or non-amyloid aggregation pathway. At acidic condition the amyloid aggregates form during the heating cycle leading to the formation of transparent hydrogel. On the contrary, in neutral condition the amyloid aggregates never form. Information on the secondary structure conformational change of ß-lactoglobulin and the formation of amyloid aggregates are obtained by FTIR spectroscopy and are related to the information of the structural changes localized around the aromatic amino acid sites by UVRR technique. Our results highlight a strong involvement of the chain portions where tryptophan is located on the formation of amyloid aggregates.