Cargando…
Manganese Ion-Induced Amyloid Fibrillation Kinetics of Hen Egg White-Lysozyme in Thermal and Acidic Conditions
[Image: see text] As manganese ions (Mn(2+)) are identified as an environmental risk factor for neurodegenerative diseases, uncovering their action mechanism on protein amyloid fibril formation is crucial for related disease treatments. Herein, we performed a combined study of Raman spectroscopy, at...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10173442/ https://www.ncbi.nlm.nih.gov/pubmed/37179629 http://dx.doi.org/10.1021/acsomega.3c01531 |
_version_ | 1785039818417242112 |
---|---|
author | Chen, Xiaodong Xing, Lei Li, Xinfei Chen, Ning Liu, Liming Wang, Jionghan Zhou, Xiaoguo Liu, Shilin |
author_facet | Chen, Xiaodong Xing, Lei Li, Xinfei Chen, Ning Liu, Liming Wang, Jionghan Zhou, Xiaoguo Liu, Shilin |
author_sort | Chen, Xiaodong |
collection | PubMed |
description | [Image: see text] As manganese ions (Mn(2+)) are identified as an environmental risk factor for neurodegenerative diseases, uncovering their action mechanism on protein amyloid fibril formation is crucial for related disease treatments. Herein, we performed a combined study of Raman spectroscopy, atomic force microscopy (AFM), thioflavin T (ThT) fluorescence, and UV–vis absorption spectroscopy assays, in which the distinctive effect of Mn(2+) on the amyloid fibrillation kinetics of hen egg white-lysozyme (HEWL) was clarified at the molecular level. With thermal and acid treatments, the unfolding of protein tertiary structures is efficiently accelerated by Mn(2+) to form oligomers, as indicated by two Raman markers for the Trp residues on protein side chains: the FWHM at 759 cm(–1) and the I(1340)/I(1360) ratio. Meanwhile, the inconsistent evolutionary kinetics of the two indicators, as well as AFM images and UV–vis absorption spectroscopy assays, validate the tendency of Mn(2+) toward the formation of amorphous aggregates instead of amyloid fibrils. Moreover, Mn(2+) plays an accelerator role in the secondary structure transition from α-helix to organized β-sheet structures, as indicated by the N–C(α)-C intensity at 933 cm(–1) and the amide I position of Raman spectroscopy and ThT fluorescence assays. Notably, the more significant promotion effect of Mn(2+) on the formation of amorphous aggregates provides credible clues to understand the fact that excess exposure to manganese is associated with neurological diseases(.) |
format | Online Article Text |
id | pubmed-10173442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-101734422023-05-12 Manganese Ion-Induced Amyloid Fibrillation Kinetics of Hen Egg White-Lysozyme in Thermal and Acidic Conditions Chen, Xiaodong Xing, Lei Li, Xinfei Chen, Ning Liu, Liming Wang, Jionghan Zhou, Xiaoguo Liu, Shilin ACS Omega [Image: see text] As manganese ions (Mn(2+)) are identified as an environmental risk factor for neurodegenerative diseases, uncovering their action mechanism on protein amyloid fibril formation is crucial for related disease treatments. Herein, we performed a combined study of Raman spectroscopy, atomic force microscopy (AFM), thioflavin T (ThT) fluorescence, and UV–vis absorption spectroscopy assays, in which the distinctive effect of Mn(2+) on the amyloid fibrillation kinetics of hen egg white-lysozyme (HEWL) was clarified at the molecular level. With thermal and acid treatments, the unfolding of protein tertiary structures is efficiently accelerated by Mn(2+) to form oligomers, as indicated by two Raman markers for the Trp residues on protein side chains: the FWHM at 759 cm(–1) and the I(1340)/I(1360) ratio. Meanwhile, the inconsistent evolutionary kinetics of the two indicators, as well as AFM images and UV–vis absorption spectroscopy assays, validate the tendency of Mn(2+) toward the formation of amorphous aggregates instead of amyloid fibrils. Moreover, Mn(2+) plays an accelerator role in the secondary structure transition from α-helix to organized β-sheet structures, as indicated by the N–C(α)-C intensity at 933 cm(–1) and the amide I position of Raman spectroscopy and ThT fluorescence assays. Notably, the more significant promotion effect of Mn(2+) on the formation of amorphous aggregates provides credible clues to understand the fact that excess exposure to manganese is associated with neurological diseases(.) American Chemical Society 2023-04-27 /pmc/articles/PMC10173442/ /pubmed/37179629 http://dx.doi.org/10.1021/acsomega.3c01531 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Chen, Xiaodong Xing, Lei Li, Xinfei Chen, Ning Liu, Liming Wang, Jionghan Zhou, Xiaoguo Liu, Shilin Manganese Ion-Induced Amyloid Fibrillation Kinetics of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title | Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title_full | Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title_fullStr | Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title_full_unstemmed | Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title_short | Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions |
title_sort | manganese ion-induced
amyloid fibrillation kinetics
of hen egg white-lysozyme in thermal and acidic conditions |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10173442/ https://www.ncbi.nlm.nih.gov/pubmed/37179629 http://dx.doi.org/10.1021/acsomega.3c01531 |
work_keys_str_mv | AT chenxiaodong manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT xinglei manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT lixinfei manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT chenning manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT liuliming manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT wangjionghan manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT zhouxiaoguo manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions AT liushilin manganeseioninducedamyloidfibrillationkineticsofheneggwhitelysozymeinthermalandacidicconditions |