{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["113(2)"],"submitter":["Yang D"],"pubmed_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."],"journal":["Peptide science (Hoboken, N.J.)"],"pagination":["e24173"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9017786"],"repository":["biostudies-literature"],"pubmed_title":["Enzymatically Forming Cell Compatible Supramolecular Assemblies of Tryptophan-Rich Short Peptides."],"pmcid":["PMC9017786"],"pubmed_authors":["Xu B","He H","Yang D","Kim BJ"],"additional_accession":[]},"is_claimable":false,"name":"Enzymatically Forming Cell Compatible Supramolecular Assemblies of Tryptophan-Rich Short Peptides.","description":"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.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2025-04-05T11:53:38.22Z","creation":"2025-02-19T04:57:58.257Z"},"accession":"S-EPMC9017786","cross_references":{"pubmed":["35445163"],"doi":["10.1002/pep2.24173"]}}