π-System Functionalization Transforms Amyloidogenic Peptide Fragment of Human Islet Amyloid Polypeptide into a Super Hydrogelator.
Chem Asian J
; 18(4): e202201235, 2023 Feb 14.
Article
em En
| MEDLINE
| ID: mdl-36567257
ABSTRACT
While a considerable number of ultra-short/short amyloid peptides have been reported to form 3D supramolecular hydrogels, they all possess high minimum gelation concentration (MGC) (≥1â
wt%), which preclude their applications. In this context, we demonstrate that functionalisation of a well-known amyloidogenic ultra-short peptide fragment NFGAIL (IAPf) of human Islet amyloid polypeptide with a π-system (Fluorenyl, Fm) at the N-terminus of the peptide (Fm-IAPf) yield not only highly thermostable hydrogel at physiological pH but also exhibited super gelator nature as the MGC (0.08â
wt%) falls below 0.1â
wt%. Various experimental results confirmed that aromatic π-π interactions from fluorenyl moieties and hydrogen bonding interactions between the IAPf drive the self-assembly/fibril formation. Fm-IAPf is the first super hydrogelator derived from amyloid-based ultra-short peptides, to the best of our knowledge. We strongly believe that this report, i. e., functionalization of an amyloid peptide with π-system, provides a lead to develop super hydrogelators from other amyloid-forming peptide fragments for their potential applications.
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Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Polipeptídeo Amiloide das Ilhotas Pancreáticas
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article