Decoupling Charge and Side Chain Effects in Hierarchical Organization of Cationic PFX Peptide and Alginate.
Biomacromolecules
; 25(7): 4168-4176, 2024 Jul 08.
Article
em En
| MEDLINE
| ID: mdl-38902961
ABSTRACT
We have successfully created self-assembled membranes by combining positively charged (Pro-X-(Phe-X)5-Pro) PFX peptides with negatively charged alginate. These PFX/alginate membranes were formed by three different peptides that contain either X = Arginine (R), Histidine (H), or Ornithine (O) as their charged amino acid. The assemblies were compared to membranes that were previously reported by us composed of X = lysine (K). This study enabled us to elucidate the impact of amino acids' specific interactions on membrane formation. SEM, SAXS, and cryo-TEM measurements show that although K, R, H, and O may have a similar net charge, the specific traits of the charged amino acid is an essential factor in determining the hierarchical structure of alginate/PFX self-assembled membranes.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alginatos
Idioma:
En
Revista:
Biomacromolecules
Ano de publicação:
2024
Tipo de documento:
Article