{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lin YA"],"funding":["NCRR NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["1419-27"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3993905"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(4)"],"pubmed_abstract":["One-dimensional nanostructures formed by self-assembly of small molecule peptides have been extensively explored for use as biomaterials in various biomedical contexts. However, unlike individual peptides that can be designed to be specifically degradable by enzymes/proteases of interest, their self-assembled nanostructures, particularly those rich in β-sheets, are generally resistant to enzymatic degradation because the specific cleavage sites are often embedded inside the nanostructures. We report here on the rational design of β-sheet rich supramolecular filaments that can specifically dissociate into less stable micellar assemblies and monomers upon treatment with matrix metalloproteases-2 (MMP-2). Through linkage of an oligoproline segment to an amyloid-derived peptide sequence, we fi"],"journal":["Biomacromolecules"],"pubmed_title":["Rational design of MMP degradable peptide-based supramolecular filaments."],"pmcid":["PMC3993905"],"funding_grant_id":["P41 RR007707","P41RR007707","T32 CA130840","P41 GM103543","R24 GM111072","R25 CA153952","P41GM103543","T-32CA130840"],"pubmed_authors":["Cui H","Ou YC","Cheetham AG","Lin YA"],"additional_accession":[]},"is_claimable":false,"name":"Rational design of MMP degradable peptide-based supramolecular filaments.","description":"One-dimensional nanostructures formed by self-assembly of small molecule peptides have been extensively explored for use as biomaterials in various biomedical contexts. However, unlike individual peptides that can be designed to be specifically degradable by enzymes/proteases of interest, their self-assembled nanostructures, particularly those rich in β-sheets, are generally resistant to enzymatic degradation because the specific cleavage sites are often embedded inside the nanostructures. We report here on the rational design of β-sheet rich supramolecular filaments that can specifically dissociate into less stable micellar assemblies and monomers upon treatment with matrix metalloproteases-2 (MMP-2). Through linkage of an oligoproline segment to an amyloid-derived peptide sequence, we fi","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2025-04-18T19:34:41.116Z","creation":"2019-03-27T01:26:49Z"},"accession":"S-EPMC3993905","cross_references":{"pubmed":["24611531"],"doi":["10.1021/bm500020j"]}}