Raman Spectroscopy Study of Skin Biopsies from Patients with Parkinson’s Disease: Trends in Alpha-Synuclein Aggregation from the Amide I Region

Author:

León-Bejarano Fabiola1,Méndez Martín O.12,Alba Alfonso12,Rodríguez-Leyva Ildefonso3,González Francisco J.4ORCID,Rodríguez-Aranda María del Carmen4,Guevara Edgar45,Guirado-López Ricardo A.6,Ramírez-Elías Miguel G.1ORCID

Affiliation:

1. Facultad de Ciencias, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

2. Laboratorio Nacional CI3M, Facultad de Ciencias, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

3. Facultad de Medicina, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

4. Coordinación para la Innovación y Aplicación de la Ciencia y la Tecnología (CIACyT), Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

5. CONACYT-Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

6. Instituto de Física, Universidad Autónoma de San Luis Potosí, San Luis Potosí, México

Abstract

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.

Funder

Consejo Nacional de Ciencia y Tecnología

Universidad Autónoma de San Luis Potosí

Publisher

SAGE Publications

Subject

Spectroscopy,Instrumentation

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