Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Pignataro MF, Herrera MG, Dodero VI (2020)
Molecules 25(20): 4854.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
OA 4.08 MB
Autor*in
Pignataro, Maria Florencia; Herrera, Maria Georgina; Dodero, Veronica IsabelUniBi
Abstract / Bemerkung
The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson's disease and Alzheimer's disease, among other aggregopathies. As a consequence, significant research efforts are directed towards the understanding of this process. In this review, we are focused on the use of UV-Visible Absorption Spectroscopy, Fluorescence Spectroscopy and Circular Dichroism to evaluate the self-organization of proteins and peptides in solution. These spectroscopic techniques are commonly available in most chemistry and biochemistry research laboratories, and together they are a powerful approach for initial as well as routine evaluation of protein and peptide self-assembly and aggregation under different environmental stimulus. Furthermore, these spectroscopic techniques are even suitable for studying complex systems like those in the food industry or pharmaceutical formulations, providing an overall idea of the folding, self-assembly, and aggregation processes, which is challenging to obtain with high-resolution methods. Here, we compiled and discussed selected examples, together with our results and those that helped us better to understand the process of protein and peptide aggregation. We put particular emphasis on the basic description of the methods as well as on the experimental considerations needed to obtain meaningful information, to help those who are just getting into this exciting area of research. Moreover, this review is particularly useful to those out of the field who would like to improve reproducibility in their cellular and biomedical experiments, especially while working with peptide and protein systems as an external stimulus. Our final aim is to show the power of these low-resolution techniques to improve our understanding of the self-assembly of peptides and proteins and translate this fundamental knowledge in biomedical research or food applications.
Erscheinungsjahr
2020
Zeitschriftentitel
Molecules
Band
25
Ausgabe
20
Art.-Nr.
4854
eISSN
1420-3049
Finanzierungs-Informationen
Open-Access-Publikationskosten wurden durch die Universität Bielefeld gefördert.
Page URI
https://pub.uni-bielefeld.de/record/2948412

Zitieren

Pignataro MF, Herrera MG, Dodero VI. Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods. Molecules. 2020;25(20): 4854.
Pignataro, M. F., Herrera, M. G., & Dodero, V. I. (2020). Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods. Molecules, 25(20), 4854. doi:10.3390/molecules25204854
Pignataro, M. F., Herrera, M. G., and Dodero, V. I. (2020). Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods. Molecules 25:4854.
Pignataro, M.F., Herrera, M.G., & Dodero, V.I., 2020. Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods. Molecules, 25(20): 4854.
M.F. Pignataro, M.G. Herrera, and V.I. Dodero, “Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods”, Molecules, vol. 25, 2020, : 4854.
Pignataro, M.F., Herrera, M.G., Dodero, V.I.: Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods. Molecules. 25, : 4854 (2020).
Pignataro, Maria Florencia, Herrera, Maria Georgina, and Dodero, Veronica Isabel. “Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods”. Molecules 25.20 (2020): 4854.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Creative Commons Namensnennung 4.0 International Public License (CC-BY 4.0):
Volltext(e)
Access Level
OA Open Access
Zuletzt Hochgeladen
2021-01-29T12:30:58Z
MD5 Prüfsumme
b3ced1492d056c395abd5ce2031f8862

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 33096797
PubMed | Europe PMC

Suchen in

Google Scholar