Clues to the Design of Aggregation-Resistant Insulin from Proline Scanning of Highly Amyloidogenic Peptides Derived from the N-Terminal Segment of the A-Chain.

A-chain amyloid insulin aggregation insulin receptor proline scan

Journal

Molecular pharmaceutics
ISSN: 1543-8392
Titre abrégé: Mol Pharm
Pays: United States
ID NLM: 101197791

Informations de publication

Date de publication:
25 Mar 2024
Historique:
medline: 25 3 2024
pubmed: 25 3 2024
entrez: 25 3 2024
Statut: aheadofprint

Résumé

Insulin aggregation poses a significant problem in pharmacology and medicine as it occurs during prolonged storage of the hormone and

Identifiants

pubmed: 38525800
doi: 10.1021/acs.molpharmaceut.4c00077
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Wojciech Puławski (W)

Bioinformatics Laboratory, Mossakowski Medical Research Institute, Polish Academy of Sciences, Pawinski Street 5, 02-106 Warsaw, Poland.

Robert Dec (R)

Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Pasteur Street 1, 02-093 Warsaw, Poland.

Wojciech Dzwolak (W)

Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Pasteur Street 1, 02-093 Warsaw, Poland.

Classifications MeSH