Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis.
S100A9
atomic force microscopy
biomolecular processes
fibril topography
mechanical properties
oligomerization
protein fibrils
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
31 Aug 2024
31 Aug 2024
Historique:
received:
29
07
2024
revised:
13
08
2024
accepted:
14
08
2024
medline:
28
9
2024
pubmed:
28
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography. Here, we use AFM to study the aggregation process of protein S100A9 in physiological conditions, in the presence of calcium at a molar ratio 4Ca
Identifiants
pubmed: 39334857
pii: biom14091091
doi: 10.3390/biom14091091
pii:
doi:
Substances chimiques
Amyloid
0
Calgranulin B
0
Calcium
SY7Q814VUP
S100A9 protein, human
0
Protein Aggregates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Fundação para a Ciência e a Tecnologia
ID : UIDB/04046/2020
Organisme : Fundação para a Ciência e a Tecnologia
ID : CEECIND/00031/2017/CP1387/CT0028
Organisme : Eurepean Union
ID : GA 215 10107914