ArticlePeptide science (Hoboken, N.J.)2021
Enzymatically Forming Cell Compatible Supramolecular Assemblies of Tryptophan-Rich Short Peptides.
Article in Peptide science (Hoboken, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Directed discovery of high-loading nanoaggregates enabled by drug-matched oligo-peptide excipients.Chem · 2025Article
- Enzyme-Instructed Intracellular Peptide Assemblies.Accounts of chemical research · 2023Article
- Synthesis and bioactivity of pyrrole-conjugated phosphopeptides.Beilstein journal of organic chemistry · 2022Article
- Enzymatic Noncovalent Synthesis.Chemical reviews · 2020Review
- Biomaterials based on noncovalent interactions of small molecules.EXCLI journal · 2020Review
- Enzyme-instructed self-assembly of the stereoisomers of pentapeptides to form biocompatible supramolecular hydrogels.Journal of drug targetingArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Here we report a new type of tryptophan-rich short peptides, which act as hydrogelators, form supramolecular assemblies via enzymatic dephosphorylation, and exhibit cell compatibility. The facile synthesis of the peptides starts with the production of phosphotyrosine, then uses solid phase peptide synthesis (SPPS) to build the phosphopeptides that contain multiple tryptophan residues. Besides exhibiting excellent solubility, these phosphopeptides, unlike the previously reported cytotoxic phenylalanine-rich phosphopeptides, are largely compatible toward mammalian cells. Our preliminary mechanistic study suggests that the tryptophan-rich peptides, instead of forming pericellular assemblies, largely accumulate in lysosomes. Such lysosomal localization may account for their cell compatibility. Moreover, these tryptophan-rich peptides are able to transiently reduce the cytotoxicity of phenylalanine-rich peptide assemblies. This rather unexpected result implies that tryptophan may act as a useful aromatic building block for developing cell compatible supramolecular assemblies for soft materials and find applications for protecting cells from cytotoxic peptide assemblies.
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Registered trials
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