eprintid: 10199431
rev_number: 9
eprint_status: archive
userid: 699
dir: disk0/10/19/94/31
datestamp: 2024-11-04 11:38:09
lastmod: 2024-11-04 11:38:09
status_changed: 2024-11-04 11:38:09
type: article
metadata_visibility: show
sword_depositor: 699
creators_name: Ayrton, John-Paul
creators_name: Ho, Chapman
creators_name: Zhang, Haoran
creators_name: Chudasama, Vijay
creators_name: Frank, Stefanie
creators_name: Thomas, Michael R
title: Multivalent nanobody engineering for enhanced physisorption and functional display on gold nanoparticles
ispublished: pub
divisions: UCL
divisions: B04
divisions: C06
divisions: F47
divisions: F56
divisions: F64
keywords: Science & Technology, Physical Sciences, Technology, Chemistry, Multidisciplinary, Nanoscience & Nanotechnology, Materials Science, Multidisciplinary, Physics, Applied, Chemistry, Science & Technology - Other Topics, Materials Science, Physics, COLLOIDAL STABILITY, GENERATION, ANTIBODIES
note: This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
abstract: The ease of expression and engineering of single domain antibodies, known as nanobodies, make them attractive alternatives to conventional antibodies in point-of-care diagnostics such as lateral flow assays. In lateral flow assays, gold nanoparticle bioconjugates serve as labels which display affinity molecules on the gold surface. While examples of nanobody gold nanoparticle bioconjugates exist, few utilise the simple one-step approach of physisorption owing to undesirable nanoparticle aggregation and loss of functionality. Here we show that engineering nanobodies into multivalent structures can significantly enhance their functionality when physisorbed onto gold nanoparticles. This approach enables resulting bioconjugates to withstand multiple processing steps required for long-term nanoparticle storage within lateral flow assays. Specifically, we show that the trivalent version of VHHV nanobody (VHH3) against the S1 protein of SARS-CoV-2 can be immobilised onto gold nanoparticles through passive adsorption. Unlike its monovalent and bivalent nanobody counterparts, using VHHV3 preserves nanoparticle stability under salt stress, blocking, washing, and freeze-drying conditions while maintaining picomolar sensitivity to the S1 protein. We anticipate that this facile strategy is a significant advancement towards the integration of nanobodies in lateral flow assay development.
date: 2024-01-01
date_type: published
publisher: ROYAL SOC CHEMISTRY
official_url: http://dx.doi.org/10.1039/d4nr02762k
oa_status: green
full_text_type: pub
language: eng
primo: open
primo_central: open_green
verified: verified_manual
elements_id: 2327559
doi: 10.1039/d4nr02762k
medium: Print-Electronic
lyricists_name: Thomas, Michael
lyricists_name: Chudasama, Vijay
lyricists_name: Frank, Stefanie
lyricists_name: Ho, Chapman
lyricists_id: MTHOA12
lyricists_id: VCHUD30
lyricists_id: SFRAN44
lyricists_id: CHOXX78
actors_name: Thomas, Michael
actors_id: MTHOA12
actors_role: owner
funding_acknowledgements: EP/T517793/1 [EPSRC]; EP/R00529X/1 [EPSRC IRC in Agile Early Warning Sensing Systems for Infectious Diseases and Antimicrobial Resistance grant]; EP/Y530542/1 [DHSC/EPSRC]
full_text_status: public
publication: Nanoscale
volume: 16
pagerange: 19881-19896
pages: 16
event_location: England
issn: 2040-3364
citation:        Ayrton, John-Paul;    Ho, Chapman;    Zhang, Haoran;    Chudasama, Vijay;    Frank, Stefanie;    Thomas, Michael R;      (2024)    Multivalent nanobody engineering for enhanced physisorption and functional display on gold nanoparticles.                   Nanoscale , 16    pp. 19881-19896.    10.1039/d4nr02762k <https://doi.org/10.1039/d4nr02762k>.       Green open access   
 
document_url: https://discovery.ucl.ac.uk/id/eprint/10199431/7/Thomas_d4nr02762k.pdf