Peptide 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 wit...
Saved in:
Main Authors: | , , , , , , , , , , , , , , , , , |
---|---|
Other Authors: | |
Format: | Article |
Language: | English |
Published: |
2022
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/163570 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
id |
sg-ntu-dr.10356-163570 |
---|---|
record_format |
dspace |
spelling |
sg-ntu-dr.10356-1635702023-07-14T16:04:40Z Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing Jin, Zhicheng Li, Yi Li, Ke Zhou, Jiajing Yeung, Justin Ling, Chuxuan Yim, Wonjun He, Tengyu Cheng, Yong Xu, Ming Creyer, Matthew N. Chang, Yu-Ci Fajtová, Pavla Retout, Maurice Qi, Baiyan Li, Shuzhou O'Donoghue, Anthony J. Jokerst, Jesse V. School of Materials Science and Engineering Institute of Materials Research and Engineering, A*STAR Engineering::Materials Main Protease Colorimetric Test 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. Resultsshow the strong aggregation propensity of the FFPC tail without polar DDD head. The SLPs were specific to the target protease, i.e., Mpro, a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses Mproin 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. Submitted/Accepted version The authors thank internal funding from the UC Office of the President (R00RG2515) and the National Institutes of Health (R01 DE031114; R21 AG065776-S1; R21 AI157957) for financial support. This work was also supported by National Science Foundation (DMR-2011924) via equipment in the UC San Diego Materials Research Science and Engineering Center (UCSD MRSEC). M.N.C. was supported by NIT under T32 CA15391.M.R. acknowledges the Wallonie-Bruxelles International (WBI) of the Fédération Wallonie-Bruxelles for financial support. The electron microscopy work was performed in part at the San Diego Nanotechnology Infrastructure (SDNI) of University of California San Diego, a member of the National Nanotechnology Coordinated Infrastructure (NNCI), which is supported by the National Science Foundation (Grant ECCS-1542148). The MANTA analysis work was supported by the National Institutes of Health (S10 OD023555). 2022-12-09T07:38:27Z 2022-12-09T07:38:27Z 2022 Journal Article Jin, Z., Li, Y., Li, K., Zhou, J., Yeung, J., Ling, C., Yim, W., He, T., Cheng, Y., Xu, M., Creyer, M. N., Chang, Y., Fajtová, P., Retout, M., Qi, B., Li, S., O'Donoghue, A. J. & Jokerst, J. V. (2022). Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing. Angewandte Chemie International Edition. https://dx.doi.org/10.1002/ange.202214394 1433-7851 https://hdl.handle.net/10356/163570 10.1002/ange.202214394 en Angewandte Chemie International Edition © 2022 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. All rights reserved. This is the peer reviewed version of the following article: Jin, Z., Li, Y., Li, K., Zhou, J., Yeung, J., Ling, C., Yim, W., He, T., Cheng, Y., Xu, M., Creyer, M. N., Chang, Y., Fajtová, P., Retout, M., Qi, B., Li, S., O'Donoghue, A. J. & Jokerst, J. V. (2022). Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing. Angewandte Chemie International Edition, which has been published in final form at https://doi.org/10.1002/ange.202214394. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. application/pdf |
institution |
Nanyang Technological University |
building |
NTU Library |
continent |
Asia |
country |
Singapore Singapore |
content_provider |
NTU Library |
collection |
DR-NTU |
language |
English |
topic |
Engineering::Materials Main Protease Colorimetric Test |
spellingShingle |
Engineering::Materials Main Protease Colorimetric Test Jin, Zhicheng Li, Yi Li, Ke Zhou, Jiajing Yeung, Justin Ling, Chuxuan Yim, Wonjun He, Tengyu Cheng, Yong Xu, Ming Creyer, Matthew N. Chang, Yu-Ci Fajtová, Pavla Retout, Maurice Qi, Baiyan Li, Shuzhou O'Donoghue, Anthony J. Jokerst, Jesse V. 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)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. Resultsshow the strong aggregation propensity of the FFPC tail without polar DDD head. The SLPs were specific to the target protease, i.e., Mpro, a biomarker for SARS-CoV-2. This system is a simple and visual tool that senses Mproin 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. |
author2 |
School of Materials Science and Engineering |
author_facet |
School of Materials Science and Engineering Jin, Zhicheng Li, Yi Li, Ke Zhou, Jiajing Yeung, Justin Ling, Chuxuan Yim, Wonjun He, Tengyu Cheng, Yong Xu, Ming Creyer, Matthew N. Chang, Yu-Ci Fajtová, Pavla Retout, Maurice Qi, Baiyan Li, Shuzhou O'Donoghue, Anthony J. Jokerst, Jesse V. |
format |
Article |
author |
Jin, Zhicheng Li, Yi Li, Ke Zhou, Jiajing Yeung, Justin Ling, Chuxuan Yim, Wonjun He, Tengyu Cheng, Yong Xu, Ming Creyer, Matthew N. Chang, Yu-Ci Fajtová, Pavla Retout, Maurice Qi, Baiyan Li, Shuzhou O'Donoghue, Anthony J. Jokerst, Jesse V. |
author_sort |
Jin, Zhicheng |
title |
Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing |
title_short |
Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing |
title_full |
Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing |
title_fullStr |
Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing |
title_full_unstemmed |
Peptide Amphiphile Mediated Co‐assembly for Nanoplasmonic Sensing |
title_sort |
peptide amphiphile mediated co‐assembly for nanoplasmonic sensing |
publishDate |
2022 |
url |
https://hdl.handle.net/10356/163570 |
_version_ |
1773551300064051200 |