Jump to main content
Jump to site search

Issue 2, 2011
Previous Article Next Article

Kinetic investigation of bioresponsive nanoparticle assembly as a function of ligand design

Author affiliations

Abstract

Homogeneous and heterogeneous nanoparticle (NP) assembly induced by ligand-specific immunorecognition is commonly used for biosensing applications. We investigated how the structural design of the peptide ligands used to functionalise gold NPs affected the kinetics of NP assembly and hence biodetection. We observed that aggregation rates varied up to 20-fold for the surface binding and 120-fold for the solution-phase assembly of NPs as a function of peptide design. Our results show how the fundamental difference in NP assembly on surfaces and in solution requires different optimised ligand designs. This increased understanding of the specifics of ligand-triggered NP aggregation should help in the design of faster and more efficient bioassays in the future.

Graphical abstract: Kinetic investigation of bioresponsive nanoparticle assembly as a function of ligand design

Back to tab navigation

Supplementary files

Publication details

The article was received on 07 Jul 2010, accepted on 28 Jul 2010 and first published on 23 Aug 2010


Article type: Communication
DOI: 10.1039/C0NR00469C
Citation: Nanoscale, 2011,3, 383-386
  •   Request permissions

    Kinetic investigation of bioresponsive nanoparticle assembly as a function of ligand design

    H. Andresen, S. Gupta and M. M. Stevens, Nanoscale, 2011, 3, 383
    DOI: 10.1039/C0NR00469C

Search articles by author

Spotlight

Advertisements