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A switch in N-terminal capping of β-peptides creates novel self-assembled nanoparticles.

ABSTRACT: Small tripeptides composed entirely of β³-amino acids have been shown to self-assemble into fibres following acylation of the N-terminus. Given the use of Fmoc as a strategy to initiate self-assembly in α-peptides, we hypothesized that the acyl cap can be replaced by an Fmoc without perturbation to the self-assembly and enable simpler synthetic protocols. We therefore replaced the N-acyl cap for an Fmoc group and herein we show that these Fmoc-protected β³-peptides produce regular spherical particles, rather than fibrous structures, that are stable and capable of encapsulating cargo. We then demonstrated that these particles were able to deliver cargo to cells without any obvious signs of cytotoxicity. This is the first description of such regular nanoparticles derived from Fmoc-protected β³-peptides.

SUBMITTER: Chen YK

PROVIDER: S-EPMC10561372 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

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A switch in N-terminal capping of β-peptides creates novel self-assembled nanoparticles.

Chen Yi-Kai YK Simon Isabella A IA Maslov Ivan I Oyarce-Pino Ivan E IE Kulkarni Ketav K Hopper Denham D Aguilar Marie-Isabel MI Vankadari Naveen N Broughton Brad Rs BR Del Borgo Mark P MP

RSC advances 20231009 42

Small tripeptides composed entirely of β3-amino acids have been shown to self-assemble into fibres following acylation of the N-terminus. Given the use of Fmoc as a strategy to initiate self-assembly in α-peptides, we hypothesized that the acyl cap can be replaced by an Fmoc without perturbation to the self-assembly and enable simpler synthetic protocols. We therefore replaced the N-acyl cap for an Fmoc group and herein we show that these Fmoc-protected β3-peptides p ...[more]

PMID: 37818265

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