| Title |
Interactions between S100A9 and alpha-synuclein: insight from NMR spectroscopy / |
| Authors |
Toleikis, Zigmantas ; Bobrovs, Raitis ; Janonienė, Agnė ; Lends, Alons ; Žiaunys, Mantas ; Baronaitė, Ieva ; Petrauskas, Vytautas ; Kitoka, Kristine ; Smirnovas, Vytautas ; Jaudzems, Kristaps |
| DOI |
10.3390/ijms23126781 |
| Full Text |
|
| Is Part of |
International journal of molecular sciences.. Basel : MDPI. 2022, vol. 23, iss. 12, art. no. 6781, p. [1-24].. eISSN 1422-0067 |
| Keywords [eng] |
AFM ; FTIR ; LDH cell toxicity tests ; MTT ; NMR ; S100A9 ; ThT fluorescence assay ; amyloid proteins ; fibrils ; synuclein |
| Abstract [eng] |
S100A9 is a pro-inflammatory protein that co-aggregates with other proteins in amyloid fibril plaques. S100A9 can influence the aggregation kinetics and amyloid fibril structure of alpha-synuclein (α-syn), which is involved in Parkinson's disease. Currently, there are limited data regarding their cross-interaction and how it influences the aggregation process. In this work, we analyzed this interaction using solution 19F and 2D 15N-1H HSQC NMR spectroscopy and studied the aggregation properties of these two proteins. Here, we show that α-syn interacts with S100A9 at specific regions, which are also essential in the first step of aggregation. We also demonstrate that the 4-fluorophenylalanine label in alpha-synuclein is a sensitive probe to study interaction and aggregation using 19F NMR spectroscopy. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2022 |
| CC license |
|
