Atomic Insight on Inhibition of Fibrillization of Dipeptides by Replacement of Phenylalanine with Tryptophan.
Journal
Langmuir : the ACS journal of surfaces and colloids
ISSN: 1520-5827
Titre abrégé: Langmuir
Pays: United States
ID NLM: 9882736
Informations de publication
Date de publication:
11 07 2023
11 07 2023
Historique:
medline:
12
7
2023
pubmed:
20
6
2023
entrez:
20
6
2023
Statut:
ppublish
Résumé
Tryptophan (Trp) conjugates destabilize amyloid fibrils responsible for amyloidoses. However, the mechanism of such destabilization is obscure. Herein the self-assembly of four synthesized Trp-containing dipeptides Boc-xxx-Trp-OMe (xxx: Val, Leu, Ile, and Phe) has been investigated and compared with the existing report on their Phe congeners. Two among them are the C-terminal tryptophan analogs of Boc-Val-Phe-OMe (VF, Aβ
Identifiants
pubmed: 37339161
doi: 10.1021/acs.langmuir.3c00823
doi:
Substances chimiques
Tryptophan
8DUH1N11BX
Phenylalanine
47E5O17Y3R
Dipeptides
0
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM