Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy

Zigmantas Toleikis; Raitis Bobrovs; Agne Janoniene; Alons Lends; Mantas Ziaunys; Ieva Baronaite; Vytautas Petrauskas; Kristine Kitoka; Vytautas Smirnovas; Kristaps Jaudzems

doi:10.3390/ijms23126781

Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy

Zigmantas Toleikis^*
, Raitis Bobrovs
, Agne Janoniene
, Alons Lends
, Mantas Ziaunys
, Ieva Baronaite
, Vytautas Petrauskas
, Kristine Kitoka
, Vytautas Smirnovas
, Kristaps Jaudzems

^*Corresponding author for this work

Latvian Institute of Organic Synthesis
Vilnius University

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

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 solution¹⁹ F and 2D¹⁵N –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 using¹⁹ F NMR spectroscopy.

Original language	English
Article number	6781
Journal	International Journal of Molecular Sciences
Volume	23
Issue number	12
DOIs	https://doi.org/10.3390/ijms23126781
Publication status	Published - 1 Jun 2022
Externally published	Yes

Keywords

AFM
FTIR
LDH cell toxicity tests
MTT
NMR
S100A9
ThT fluorescence assay
amyloid proteins
fibrils
synuclein

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title = "Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy",

abstract = "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{\textquoteright}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 solution19 F and 2D15N {\textendash}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 using19 F NMR spectroscopy.",

keywords = "AFM, FTIR, LDH cell toxicity tests, MTT, NMR, S100A9, ThT fluorescence assay, amyloid proteins, fibrils, synuclein",

author = "Zigmantas Toleikis and Raitis Bobrovs and Agne Janoniene and Alons Lends and Mantas Ziaunys and Ieva Baronaite and Vytautas Petrauskas and Kristine Kitoka and Vytautas Smirnovas and Kristaps Jaudzems",

note = "Publisher Copyright: {\textcopyright} 2022 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2022",

month = jun,

day = "1",

doi = "10.3390/ijms23126781",

language = "English",

volume = "23",

journal = "International Journal of Molecular Sciences",

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TY - JOUR

T1 - Interactions between S100A9 and Alpha-Synuclein

T2 - Insight from NMR Spectroscopy

AU - Toleikis, Zigmantas

AU - Bobrovs, Raitis

AU - Janoniene, Agne

AU - Lends, Alons

AU - Ziaunys, Mantas

AU - Baronaite, Ieva

AU - Petrauskas, Vytautas

AU - Kitoka, Kristine

AU - Smirnovas, Vytautas

AU - Jaudzems, Kristaps

PY - 2022/6/1

Y1 - 2022/6/1

N2 - 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 solution19 F and 2D15N –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 using19 F NMR spectroscopy.

AB - 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 solution19 F and 2D15N –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 using19 F NMR spectroscopy.

KW - AFM

KW - FTIR

KW - LDH cell toxicity tests

KW - MTT

KW - NMR

KW - S100A9

KW - ThT fluorescence assay

KW - amyloid proteins

KW - fibrils

KW - synuclein

UR - https://www.scopus.com/pages/publications/85132296342

U2 - 10.3390/ijms23126781

DO - 10.3390/ijms23126781

M3 - Article

C2 - 35743221

AN - SCOPUS:85132296342

SN - 1661-6596

VL - 23

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

IS - 12

M1 - 6781

ER -

Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy

Abstract

Keywords

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