Peptide valence-induced breaks in plasmonic coupling

Electrostatic interactions are a key driving force that mediates colloidal assembly. The Schulze-Hardy rule states that nanoparticles have a higher tendency to coagulate in the presence of counterions with high charge valence. However, it is unclear how the Schulze-Hardy rule works when the simple e...

Full description

Bibliographic Details
Main Authors: Chang, Yu-Ci, Jin, Zhicheng, Li, Ke, Zhou, Jiajing, Yim, Wonjun, Yeung, Justin, Cheng, Yong, Retout, Maurice, Creyer, Matthew N., Fajtová, Pavla, He, Tengyu, Chen, Xi, O'Donoghue, Anthony J., Jokerst, Jesse V.
Other Authors: School of Materials Science and Engineering
Format: Journal Article
Language:English
Published: 2023
Subjects:
Online Access:https://hdl.handle.net/10356/169777
_version_ 1826129063604912128
author Chang, Yu-Ci
Jin, Zhicheng
Li, Ke
Zhou, Jiajing
Yim, Wonjun
Yeung, Justin
Cheng, Yong
Retout, Maurice
Creyer, Matthew N.
Fajtová, Pavla
He, Tengyu
Chen, Xi
O'Donoghue, Anthony J.
Jokerst, Jesse V.
author2 School of Materials Science and Engineering
author_facet School of Materials Science and Engineering
Chang, Yu-Ci
Jin, Zhicheng
Li, Ke
Zhou, Jiajing
Yim, Wonjun
Yeung, Justin
Cheng, Yong
Retout, Maurice
Creyer, Matthew N.
Fajtová, Pavla
He, Tengyu
Chen, Xi
O'Donoghue, Anthony J.
Jokerst, Jesse V.
author_sort Chang, Yu-Ci
collection NTU
description Electrostatic interactions are a key driving force that mediates colloidal assembly. The Schulze-Hardy rule states that nanoparticles have a higher tendency to coagulate in the presence of counterions with high charge valence. However, it is unclear how the Schulze-Hardy rule works when the simple electrolytes are replaced with more sophisticated charge carriers. Here, we designed cationic peptides of varying valencies and demonstrate that their charge screening behaviors on anionic gold nanoparticles (AuNPs) follow the six-power relationship in the Schulze-Hardy rule. This finding further inspires a simple yet effective strategy for measuring SARS-CoV-2 main protease (Mpro) via naked eyes. This work provides a unique avenue for fundamental NP disassembly based on the Schulze-Hardy rule and can help design versatile substrates for colorimetric sensing of other proteases.
first_indexed 2024-10-01T07:34:37Z
format Journal Article
id ntu-10356/169777
institution Nanyang Technological University
language English
last_indexed 2024-10-01T07:34:37Z
publishDate 2023
record_format dspace
spelling ntu-10356/1697772023-08-04T15:45:49Z Peptide valence-induced breaks in plasmonic coupling Chang, Yu-Ci Jin, Zhicheng Li, Ke Zhou, Jiajing Yim, Wonjun Yeung, Justin Cheng, Yong Retout, Maurice Creyer, Matthew N. Fajtová, Pavla He, Tengyu Chen, Xi O'Donoghue, Anthony J. Jokerst, Jesse V. School of Materials Science and Engineering Engineering::Materials Cationic Peptides Colloidal Assembly Electrostatic interactions are a key driving force that mediates colloidal assembly. The Schulze-Hardy rule states that nanoparticles have a higher tendency to coagulate in the presence of counterions with high charge valence. However, it is unclear how the Schulze-Hardy rule works when the simple electrolytes are replaced with more sophisticated charge carriers. Here, we designed cationic peptides of varying valencies and demonstrate that their charge screening behaviors on anionic gold nanoparticles (AuNPs) follow the six-power relationship in the Schulze-Hardy rule. This finding further inspires a simple yet effective strategy for measuring SARS-CoV-2 main protease (Mpro) via naked eyes. This work provides a unique avenue for fundamental NP disassembly based on the Schulze-Hardy rule and can help design versatile substrates for colorimetric sensing of other proteases. Published version The authors thank the National Institutes of Health (R01 DE031114; R21 AG065776-S1; R21 AI157957) for financial support. The electron microscopy work was performed in part at the San Diego Nanotechnology Infrastructure (SDNI) of the University of California, San Diego, a member of the National Nanotechnology Coordinated Infrastructure (NNCI), which is supported by the National Science Foundation (Grant ECCS1542148). M. N. C. acknowledges fellowship support from T32 CA153915. All publication charges for this article have been paid for by the Royal Society of Chemistry. 2023-08-02T06:06:39Z 2023-08-02T06:06:39Z 2023 Journal Article Chang, Y., Jin, Z., Li, K., Zhou, J., Yim, W., Yeung, J., Cheng, Y., Retout, M., Creyer, M. N., Fajtová, P., He, T., Chen, X., O'Donoghue, A. J. & Jokerst, J. V. (2023). Peptide valence-induced breaks in plasmonic coupling. Chemical Science, 14(10), 2659-2668. https://dx.doi.org/10.1039/d2sc05837e 2041-6520 https://hdl.handle.net/10356/169777 10.1039/d2sc05837e 36908948 2-s2.0-85148751290 10 14 2659 2668 en Chemical Science © 2023 The Author(s). Published by the Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. application/pdf
spellingShingle Engineering::Materials
Cationic Peptides
Colloidal Assembly
Chang, Yu-Ci
Jin, Zhicheng
Li, Ke
Zhou, Jiajing
Yim, Wonjun
Yeung, Justin
Cheng, Yong
Retout, Maurice
Creyer, Matthew N.
Fajtová, Pavla
He, Tengyu
Chen, Xi
O'Donoghue, Anthony J.
Jokerst, Jesse V.
Peptide valence-induced breaks in plasmonic coupling
title Peptide valence-induced breaks in plasmonic coupling
title_full Peptide valence-induced breaks in plasmonic coupling
title_fullStr Peptide valence-induced breaks in plasmonic coupling
title_full_unstemmed Peptide valence-induced breaks in plasmonic coupling
title_short Peptide valence-induced breaks in plasmonic coupling
title_sort peptide valence induced breaks in plasmonic coupling
topic Engineering::Materials
Cationic Peptides
Colloidal Assembly
url https://hdl.handle.net/10356/169777
work_keys_str_mv AT changyuci peptidevalenceinducedbreaksinplasmoniccoupling
AT jinzhicheng peptidevalenceinducedbreaksinplasmoniccoupling
AT like peptidevalenceinducedbreaksinplasmoniccoupling
AT zhoujiajing peptidevalenceinducedbreaksinplasmoniccoupling
AT yimwonjun peptidevalenceinducedbreaksinplasmoniccoupling
AT yeungjustin peptidevalenceinducedbreaksinplasmoniccoupling
AT chengyong peptidevalenceinducedbreaksinplasmoniccoupling
AT retoutmaurice peptidevalenceinducedbreaksinplasmoniccoupling
AT creyermatthewn peptidevalenceinducedbreaksinplasmoniccoupling
AT fajtovapavla peptidevalenceinducedbreaksinplasmoniccoupling
AT hetengyu peptidevalenceinducedbreaksinplasmoniccoupling
AT chenxi peptidevalenceinducedbreaksinplasmoniccoupling
AT odonoghueanthonyj peptidevalenceinducedbreaksinplasmoniccoupling
AT jokerstjessev peptidevalenceinducedbreaksinplasmoniccoupling