{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jin Z"],"funding":["NIDCR NIH HHS","NIA NIH HHS","NIAID NIH HHS","NIH HHS","National Science Foundation"],"pagination":["e202214394"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9852014"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(4)"],"pubmed_abstract":["Aromatic interactions are commonly involved in the assembly of naturally occurring building blocks, and these interactions can be replicated in an artificial setting to produce functional materials. Here we describe a colorimetric biosensor using co-assembly experiments with plasmonic gold and surfactant-like peptides (SLPs) spanning a wide range of aromatic residues, polar stretches, and interfacial affinities. The SLPs programmed in DDD-(ZZ)<sub>x</sub> -FFPC self-assemble into higher-order structures in response to a protease and subsequently modulate the colloidal dispersity of gold leading to a colorimetric readout. Results show the strong aggregation propensity of the FFPC tail without polar DDD head. The SLPs were specific to the target protease, i.e., M<sup>pro</sup> , a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses M<sup>pro</sup> in phosphate buffer, exhaled breath condensate, and saliva with detection limits of 15.7, 20.8, and 26.1 nM, respectively. These results may have value in designing other protease testing methods."],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Peptide Amphiphile Mediated Co-assembly for Nanoplasmonic Sensing."],"pmcid":["PMC9852014"],"funding_grant_id":["S10 OD023555","R21 AG065776","ECCS-1542148","R01 DE031114","R21 DE029917","DMR-2011924","R21 AI157957"],"pubmed_authors":["Retout M","Yim W","Xu M","Yeung J","Fajtova P","Li K","Jin Z","O'Donoghue AJ","Cheng Y","Chang YC","Li Y","Ling C","He T","Creyer MN","Li S","Jokerst JV","Qi B","Zhou J"],"additional_accession":[]},"is_claimable":false,"name":"Peptide Amphiphile Mediated Co-assembly for Nanoplasmonic Sensing.","description":"Aromatic interactions are commonly involved in the assembly of naturally occurring building blocks, and these interactions can be replicated in an artificial setting to produce functional materials. Here we describe a colorimetric biosensor using co-assembly experiments with plasmonic gold and surfactant-like peptides (SLPs) spanning a wide range of aromatic residues, polar stretches, and interfacial affinities. The SLPs programmed in DDD-(ZZ)<sub>x</sub> -FFPC self-assemble into higher-order structures in response to a protease and subsequently modulate the colloidal dispersity of gold leading to a colorimetric readout. Results show the strong aggregation propensity of the FFPC tail without polar DDD head. The SLPs were specific to the target protease, i.e., M<sup>pro</sup> , a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses M<sup>pro</sup> in phosphate buffer, exhaled breath condensate, and saliva with detection limits of 15.7, 20.8, and 26.1 nM, respectively. These results may have value in designing other protease testing methods.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-03-18T14:11:46.92Z","creation":"2025-04-04T07:24:48.069Z"},"accession":"S-EPMC9852014","cross_references":{"pubmed":["36409652"],"doi":["10.1002/anie.202214394"]}}