Targeted inhibition of amyloidogenesis using a non-toxic, serum stable strategically designed cyclic peptide with therapeutic implications.
Amyloid
Inhibition
Microscopy
NMR
Raman spectroscopy
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
01
10
2019
revised:
24
01
2020
accepted:
31
01
2020
pubmed:
8
2
2020
medline:
18
7
2020
entrez:
8
2
2020
Statut:
ppublish
Résumé
Amyloidogenic disorders are currently rising as a global health issue, prompting more and more studies dedicated to the development of effective targeted therapeutics. The innate affinity of these amyloidogenic proteins towards the biomembranes adds further complexities to the systems. Our previous studies have shown that biologically active peptides can effectively target amyloidogenesis serving as an efficient therapeutic alternative in several amyloidogenic disorders. The structural uniqueness of the PWWP motif in the de novo designed heptapeptide, KR7 (KPWWPRR-NH
Identifiants
pubmed: 32032759
pii: S1570-9639(20)30019-4
doi: 10.1016/j.bbapap.2020.140378
pii:
doi:
Substances chimiques
Amyloid
0
Insulin
0
Peptides, Cyclic
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
140378Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest None.