PXD066055-1

PXD066055 is an original dataset announced via ProteomeXchange.

Title	SUMO-2 activity is inhibited by non-covalent interactions with the Aβ peptide: an exploration of potential pathogenic mechanisms in Alzheimer’s Disease
Description	SUMOylation is a post-translational modification involving the addition of SUMO isoforms to target proteins and plays a role in various biological processes, including neurodegenerative diseases and ocular pathologies. This study investigates the interaction between SUMO-2 and amyloid (Aβ) peptides, key contributors to Alzheimer’s disease, using techniques like cross-linking mass spectrometry, surface plasmon resonance and biolayer interferometry. The results show that Aβ1-40 and Aβ1-42 bind more strongly to SUMO-2 than to ubiquitin, with binding driven by specific hydrogen bonds and hydrophobic interactions. SUMO-2 was found to inhibit the conversion of Aβ into β-sheet structures and impede Aβ aggregation. Notably, Aβ competes with SUMO-2’s canonical substrates for binding, completely hindering SUMOylation reactions in vitro. Identifying SUMO-2/Aβ1-42 adducts in cellular extracts and live cells further highlights the biological significance of these interactions. Overall, the findings indicate that Aβ peptides impair SUMO-2 function, pointing to the necessity for more research on the implications of SUMOylation in Alzheimer's disease.
HostingRepository	PRIDE
AnnounceDate	2025-08-25
AnnouncementXML	Submission_2025-08-24_17:16:48.381.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alessio Di Ianni
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2025-07-11 05:32:14	ID requested
⏵ 1	2025-08-24 17:16:50	announced

10.1016/j.ijbiomac.2025.146632;

Ciaffaglione V, Grasso G, Lanza V, Sciacca MFM, Zimbone S, Giuffrida ML, Iacobucci C, Di Ianni A, Calcagno D, Grasso G, Alloni A, Orsini F, Fraser P, Fioriti L, Milardi D, peptide: an exploration of potential pathogenic mechanisms in Alzheimer's disease. Int J Biol Macromol, 323(Pt 1):146632(2025) [pubmed]

submitter keyword: Aβ, protein protein interactions, Crosslinking MS, Alzheimer’s Disease, XL-MS,SUMO-2, Cross-linking mass spectrometry

Danilo milardi
contact affiliation	Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Sede Secondaria di Catania, Via Paolo Gaifami 18, 95126 Catania, Italy
contact email	danilo.milardi@cnr.it
lab head
Alessio Di Ianni
contact affiliation	Human Technopole
contact email	alessio.diianni@fht.org
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/08/PXD066055

PRIDE project URI

• PRIDE
  1. PXD066055
     1. Label: PRIDE project
     2. Name: SUMO-2 activity is inhibited by non-covalent interactions with the Aβ peptide: an exploration of potential pathogenic mechanisms in Alzheimer’s Disease