Deposition of misfolded proteins as extracellular amyloid aggregates is the pathological hallmark of systemic amyloidoses. Subcutaneous fat acquired by fine needle aspiration is the preferred screening tissue in suspected patients. In this study we employed Fourier transform infrared (FTIR) spectroscopy in attenuated total reflection (ATR) to investigate human abdominal fat aspirates with the aim of detecting disease-related changes in the molecular structure and composition of the tissue and exploiting the potentiality of the method to discriminate between amyloid-positive and -negative samples. The absorption and second-derivative spectra of Congo Red (CR) positive and CR-negative specimens were analyzed by three multivariate methods in four spectral regions. The proposed ATR-FTIR method is label-free, rapid, and relatively inexpensive and requires minimal sample preparation. We found that the ATR-FTIR approach can differentiate fat aspirates containing amyloid deposits from control specimens with high sensitivity and specificity, both at 100 [89-100]%. It is worth noting that the wavenumbers most important for discrimination indicate that changes both in the protein conformation and in resident lipids are intrinsic features of affected subcutaneous fat in comparison with the CR-negative controls. In this proof of concept study, we show that this approach could be useful for assessing tissue amyloid aggregates and for acquiring novel knowledge of the molecular bases of the disease.
ASJC Scopus subject areas
- Analytical Chemistry