Self-assembled aggregates based on cationic amphiphilic peptides: structural insight

Autor(es)

Rosa, Elisabetta ; Diaferia, Carlo ; De Mello, Lucas ; Seitsonen, Jani ; Hamley, Ian W. ; Accardo, Antonella

• Tipo de documento: Artigo Científico
• Fonte: SOFT MATTER; v. 19, n. 25, p. 11-pg., 2023-05-23.

Resumo

Short and ultra-short peptides have recently emerged as suitable building blocks for the fabrication of self-assembled innovative materials. Peptide aggregation is strictly related to the amino acids composing the sequence and their capability to establish intermolecular interactions. Additional structural and functional properties can also be achieved by peptide derivatization (e.g. with polymeric moieties, alkyl chains or other organic molecules). For instance, peptide amphiphiles (PAs), containing one or more alkyl tails on the backbone, have a propensity to form highly ordered nanostructures like nanotapes, twisted helices, nanotubes and cylindrical nanostructures. Further lateral interactions among peptides can also promote hydrogelation. Here we report the synthesis and the aggregation behaviour of four PAs containing cationic tetra- or hexa-peptides (C-19-VAGK, C-19-K1, C-19-K2 and C-19-K3) derivatized with a nonadecanoic alkyl chain. In their acetylated (Ac-) or fluorenylated (Fmoc-) versions, these peptides previously demonstrated the ability to form biocompatible hydrogels potentially suitable as extracellular matrices for tissue engineering or diagnostic MRI applications. In the micromolar range, PAs self-assemble in aqueous solution into nanotapes, or small clusters, resulting in high biocompatibility on HaCat cells up to 72 hours of incubation. Moreover, C19-VAGK also forms a gel at a concentration of 5 wt%. (AU)

• Processo FAPESP: 19/19719-1 - Matrizes peptídicas bioativas: da estrutura molecular às aplicações biomédicas
• Beneficiário: Lucas Rodrigues de Mello
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 19/20907-7 - Organização estrutural e bioatividade em sistemas auto-organizados de peptídeos e nucleotídeos
• Beneficiário: Emerson Rodrigo da Silva
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 21/10092-6 - Desenvolvimento de matrizes peptídicas bioativas: da estrutura molecular às aplicações biomédicas
• Beneficiário: Lucas Rodrigues de Mello
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Doutorado