Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides.
Soft Matter
; 16(20): 4800-4805, 2020 May 28.
Article
em En
| MEDLINE
| ID: mdl-32400837
ABSTRACT
Peptide hydrogels show great promise as extracellular matrix mimics due to their tuneable, fibrous nature. Through incorporation of polar cationic, polar anionic or polar neutral amino acids into the Fmoc-diphenylalanine motif, we show that electrostatic charge plays a key role in the properties of the subsequent gelators. Specifically, we show that an inverse relationship exists for biocompatibility in the solution state versus the gel state for cationic and anionic peptides. Finally, we use tethered bilayer lipid membrane (tBLM) experiments to suggest a likely mode of cytotoxicity for tetrapeptides which exhibit cytotoxicity in the solution state.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Hidrogéis
/
Fluorenos
/
Aminoácidos
Limite:
Humans
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article