ABSTRACT
Excess fat in abdominal deposits is a risk factor for multiple conditions, including metabolic syndrome (MetS); lipid metabolism plays an essential role in these pathologies; fatty acid-binding proteins (FABPs) are dedicated to the cytosolic transport of fat. FABP4, whose primary source is adipose tissue, is released into the circulation, acting as an adipokine, while FABP5 also accompanies the adverse effects of MetS. FABP4 and 5 are potential biomarkers of MetS, but their behavior during syndrome evolution has not been determined. Raman spectroscopy has been applied as an alternative method to disease biomarker detection. In this work, we detected spectral changes related to FABP4 and 5 in the serum at different points of time, using an animal model of a high-fat diet-induced MetS. FABP4 and 5 spectral changes show a contribution during the evolution of MetS, which indicates alteration to a molecular level that predisposes to established MetS. These findings place FABPs as potential biomarkers of MetS and Raman spectroscopy as an alternative method for MetS assessment.
Subject(s)
Metabolic Syndrome , Animals , Metabolic Syndrome/metabolism , Spectrum Analysis, Raman , Risk Factors , Fatty Acid-Binding Proteins/metabolism , BiomarkersABSTRACT
Parkinson's disease (PD) is one of the most common neurological pathologies with a high prevalence worldwide. PD is characterized by Lewy bodies, whose major component is the aggregates of α-synuclein (αSyn) protein. Interestingly, recent works have demonstrated that skin biopsy studies are a promising diagnostic tool for evaluating α-synucleinopathies. In this sense, this work focuses on the detection of αSyn in skin biopsies employing Raman spectroscopy, using three different approaches: (i) the in vitro Raman spectrum of α-synuclein, (ii) the ex vivo Raman spectra of human skin biopsies from healthy and Parkinson's disease patients, and (iii) theoretical calculations of the Raman spectra obtained from different model αSyn fragments using density functional theory (DFT). Significant differences in the intensity and location of Raman active frequencies in the amide I region were found when comparing healthy and PD subjects related to α-synuclein conformational changes and variations in their aggregation behavior. In samples from healthy patients, we identified well-known Raman peaks at 1655, 1664, and 1680 cm-1 associated with the normal state of the protein. In PD subjects, shifted Raman bands and intensity variations were found at 1650, 1670, and 1687 cm-1 associated with aggregated forms of the protein. DFT calculations reveal that the shape of the amide I Raman peak in model αSyn fragments strongly depends on the degree of aggregation. Sizable frequency shifts and intensity variations are found within the highly relevant 1600-1700 cm-1 domain, revealing the sensitivity of the amide I Raman band to the changes in the local atomic environment. Interestingly, we obtain that the presence of surrounding waters also affects the structure of the amide I band, leading to the appearance of new peaks on the low-frequency side and a notable broadening of the Raman spectra. These results strongly suggest that, through Raman spectroscopy, it is possible to infer the presence of aggregated forms of αSyn in skin biopsies, a result that could have important implications for understanding α-synuclein related diseases.
Subject(s)
Parkinson Disease , alpha-Synuclein , Humans , alpha-Synuclein/metabolism , Parkinson Disease/diagnosis , Parkinson Disease/metabolism , Spectrum Analysis, Raman/methods , Amides , BiopsyABSTRACT
In this paper, we report a fast and easy method to detect histamine dihydrochloride using gold nanostars in colloidal aqueous solution as a highly active SERS platform with potential applications in biomedicine and food science. This colloid was characterized with SEM and UVâ»Vis spectroscopy. Also, numerical calculations were performed to estimate the plasmonic resonance and electric field amplification of the gold nanoparticles to compare the difference between nanospheres and nanostars. Finally, aqueous solutions of histamine dihydrochloride were prepared in a wide range of concentrations and the colloid was added to carry out SERS. We found SERS amplified the Raman signal of histamine by an enhancement factor of 1 . 0 × 10 7 , demonstrating the capability of the method to detect low concentrations of this amine molecule.