Abstract
It is known that the presence of protein aggregates in biological samples is associated with natural aging processes and age-related diseases. The objective of this technical study was to evaluate the potential of Fourier Transform Infrared Spectroscopy to identify the presence of protein aggregates in Saccharomyces cerevisiae containing high levels of protein aggregates. We acquired ATR-FTIR spectra at mid-infrared range (between 4000 and 600 cm-1) and used multivariate analysis to analyze the data. Significant differences between spectra of wild type and mutant strains in the spectral range assigned to proteins were observed. In particular, an increase in β-sheet structures in mutant strains (spectral signals at 1683 and 1628 cm-1) was observed, indicating the putative presence of protein aggregates. These results prove the capacity of FTIR to evaluate changes in protein conformation, mainly protein aggregation, in a fast, simple and non-expensive way, producing insights on the possible application of this technique to the detection of protein aggregates in human biological samples.
Highlights
Life expectancy has exponentially increased in the past decades, bringing huge challenges to healthcare for the treatment of age-related diseases [1] [2] [3]
It is known that the presence of protein aggregates in biological samples is associated with natural aging processes and age-related diseases
The objective of this technical study was to evaluate the potential of Fourier Transform Infrared Spectroscopy to identify the presence of protein aggregates in Saccharomyces cerevisiae containing high levels of protein aggregates
Summary
Life expectancy has exponentially increased in the past decades, bringing huge challenges to healthcare for the treatment of age-related diseases [1] [2] [3]. The decline in proteostasis, i.e. a decrease in the activity and/or expression of the components of the unfolded protein response, is linked to the aging process [6] This leads to the accumulation of aberrant proteins that can organize into aggregates that are potentially toxic to the cell [7]. Specific protein aggregates not associated to a specific disease can be potential biomarkers of physiological aging To identify these aggregates, we need reliable methodologies that can detect changes in protein conformation in biological samples in a simple, accurate and inexpensive manner. We need reliable methodologies that can detect changes in protein conformation in biological samples in a simple, accurate and inexpensive manner Metabolomic approaches, such as Fourier Transform Infrared Spectroscopy, seem to be reliable and promising to study protein aggregation, since age-related metabolic modifications can result in structural changes that modify IR spectra [13] [14] [15]. Our data clearly indicate that FTIR can be used to detect such protein aggregates
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