FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples

Article Sidebar

27-Jan-2616.pdf
Published Feb 24, 2022
DOI: https://doi.org/10.18103/mra.v10i2.2616

Downloads

Download data is not yet available.

Main Article Content

Sandra Magalhães
iBiMED: Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal; CICECO: Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, Aveiro, Portugal
Manuel Teixeira
iBiMED: Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal
Marisol Gouveia
iBiMED: Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal
Fernando Ribeiro
iBiMED: Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal; ESSUA: School of Health Sciences, University of Aveiro, Aveiro, Portugal
Brian J Goodfellow
CICECO: Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, Aveiro, Portugal
Alexandra Nunes
iBiMED: Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal

Abstract

The loss of proteostasis is a key hallmark of aging and has been well documented using several model systems. However, in biofluids such as blood plasma, little is known about how the loss of proteostasis affects protein conformation during aging.


Our previous work has demonstrated age-related changes in protein conformation in human plasma samples using FTIR spectroscopy and conformation-specific antibodies. To prove the potential of spectroscopy to detect slight changes in protein secondary structure during aging, we have applied the same methodology to a new and independent set of 24 human plasma samples from donors with ages ranging from 40 to 75 years.


The results clearly show that from middle to old age there is a decrease in antiparallel β-sheet structures and an increase in intermolecular β-sheets, indicative of an increase in aggregation-prone proteins in human plasma over time. This confirms the potential of FTIR spectroscopy as a technique to evaluate protein conformational changes related to health and disease and as a suitable method to be used in a clinical setting to produce quick and reliable results.

Keywords: Protein conformation, Aging, FTIR spectroscopy

Article Details

How to Cite
MAGALHÃES, Sandra et al. FTIR spectroscopy confirms age-related changes in protein conformation in a new independent dataset of human plasma samples. Medical Research Archives, [S.l.], v. 10, n. 2, feb. 2022. ISSN 2375-1924. Available at: <https://esmed.org/MRA/mra/article/view/2616>. Date accessed: 20 apr. 2024. doi: https://doi.org/10.18103/mra.v10i2.2616.
ABNT APA BibTeX CBE EndNote - EndNote format (Macintosh & Windows) MLA ProCite - RIS format (Macintosh & Windows) RefWorks Reference Manager - RIS format (Windows only) Turabian
Issue
Vol 10 No 2 (2022): Vol.10 Issue 2, February, 2022
Section
Research Articles

The Medical Research Archives grants authors the right to publish and reproduce the unrevised contribution in whole or in part at any time and in any form for any scholarly non-commercial purpose with the condition that all publications of the contribution include a full citation to the journal as published by the Medical Research Archives.

 

References

1. López-Otín C, Blasco M, Partridge L, Serrano M, Kroemer G. The hallmarks of aging. Cell. 2013;153(6):1194–217.
2. Magalhães S, Goodfellow BJ, Nunes A. Aging and Proteins: What Does Proteostasis Have to Do with Age? Curr Mol Med. 2018;18(3):178–89.
3. Lewis GD, Farrell L, Wood MJ, Martinovic M, Arany Z, Rowe GC, et al. Metabolic Signatures of Exercise in Human Plasma. Sci Transl Med. 2010;2(33):33ra37.
4. Chaleckis R, Murakami I, Takada J, Kondoh H, Yanagida M. Individual variability in human blood Metabolites identifies age-related differences. Proc Natl Acad Sci U S A. 2016;113(16):4252–9.
5. Ayyadevara S, Mercanti F, Wang X, Mackintosh SG, Tackett AJ, Prayaga SVSS, et al. Age- and Hypertension-Associated Protein Aggregates in Mouse Heart Have Similar Proteomic Profiles. Hypertension. 2016 May;67(5):1006–13.
6. Tanase M, Urbanska AM, Zolla V, Clement CC, Huang L, Morozova K, et al. Role of Carbonyl Modifications on Aging-Associated Protein Aggregation. Sci Rep. 2016 May;6(1):19311.
7. Leeman DS, Hebestreit K, Ruetz T, Webb AE, McKay A, Pollina EA, et al. Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging. Science. 2018 Mar;359(6381):1277–83.
8. Finlayson D, Rinaldi C, Baker MJ. Is Infrared Spectroscopy Ready for the Clinic? Anal Chem. 2019 Oct;91(19):12117–28.
9. Magalhães S, Trindade D, Martins T, Martins Rosa I, Delgadillo I, Goodfellow BJ, et al. Monitoring plasma protein aggregation during aging using conformation-specific antibodies and FTIR spectroscopy. Clin Chim Acta. 2020;502:25–33.
10. Magalhães S, Goodfellow BJ, Nunes A. FTIR spectroscopy in biomedical research: how to get the most out of its potential. Appl Spectrosc Rev. 2021;
11. Shivu B, Seshadri S, Li J, Oberg KA, Uversky VN, Fink AL. Distinct β-Sheet Structure in Protein Aggregates Determined by ATR–FTIR Spectroscopy. Biochemistry. 2013 Aug;52(31):5176–83.
12. Asuero AG, Sayago A, González AG. The correlation coefficient: An overview. Crit Rev Anal Chem. 2006;36(1):41–59.
13. Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annu Rev Biochem. 2017 Jun;86:27–68.
14. Chiti F, Dobson CM. Protein Misfolding, Functional Amyloid, and Human Disease. Annu Rev Biochem. 2006 Jun;75:333–66.
15. Roeters SJ, Iyer A, Pletikapić G, Kogan V, Subramaniam V, Woutersen S. Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy. Sci Rep. 2017 Jan;7:41051.
16. Dong A, Huang P, Caughey WS. Protein Secondary Structures in Water from Second-Derivative Amide I Infrared Spectra. Biochemistry. 1990;29(13):3303–8.
17. Byler DM, Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 1986;25(3):469–87.
18. Bagińska K, Makowska J, Wiczk W, Kasprzykowski F, Chmurzyński L. Conformational studies of alanine-rich peptide using CD and FTIR spectroscopy. J Pept Sci. 2008;14(3):283–9.
19. Kaushik S, Cuervo AM. Proteostasis and aging. Nat Med. 2015 Dec;21(12):1406–15.
20. Wolfe KJ, Cyr DM. Amyloid in neurodegenerative diseases: Friend or foe? Semin Cell Dev Biol. 2011 Jul;22(5):476–81.