biostudies-literatureJin ZNIDCR NIH HHSNIA NIH HHSNIAID NIH HHSNIH HHSNational Science Foundatione202214394https://www.ebi.ac.uk/biostudies/studies/S-EPMC9852014biostudies-literatureUnknown62(4)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)_x -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^pro , a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses M^pro 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.Angewandte Chemie (International ed. in English)Peptide Amphiphile Mediated Co-assembly for Nanoplasmonic Sensing.PMC9852014S10 OD023555R21 AG065776ECCS-1542148R01 DE031114R21 DE029917DMR-2011924R21 AI157957Retout MYim WXu MYeung JFajtova PLi KJin ZO'Donoghue AJCheng YChang YCLi YLing CHe TCreyer MNLi SJokerst JVQi BZhou JfalsePeptide Amphiphile Mediated Co-assembly for Nanoplasmonic Sensing.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)_x -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^pro , a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses M^pro 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.2023-01-01T00:00:00Z2023 Jan2026-03-18T14:11:46.92Z2025-04-04T07:24:48.069ZS-EPMC98520143640965210.1002/anie.202214394