Elucidating the binding mechanism of a novel silica-binding peptide

Rachit Bansal, Zehra Elgundi, Andrew Care, Sophia C. Goodchild, Megan S. Lord, Alison Rodger, Anwar Sunna

Research output: Contribution to journalArticle

2 Citations (Scopus)
4 Downloads (Pure)

Abstract

Linker-protein G (LPG) is a bifunctional fusion protein composed of a solid-binding peptide (SBP, referred as the "linker") with high affinity to silica-based compounds and a Streptococcus protein G (PG), which binds antibodies. The binding mechanisms of LPG to silica-based materials was studied using different biophysical techniques and compared to that of PG without the linker. LPG displayed high binding affinity to a silica surface (KD = 34.77 ± 11.8 nM), with a vertical orientation, in comparison to parent PG, which exhibited no measurable binding affinity. Incorporation of the linker in the fusion protein, LPG, had no effect on the antibody-binding function of PG, which retained its secondary structure and displayed no alteration of its chemical stability. The LPG system provided a milder, easier, and faster affinity-driven immobilization of antibodies to inorganic surfaces when compared to traditional chemical coupling techniques.

Original languageEnglish
Article number4
Pages (from-to)1-15
Number of pages15
JournalBiomolecules
Volume10
Issue number1
DOIs
Publication statusPublished - Jan 2020

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Bibliographical note

Copyright the Author(s) 2019. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

  • solid-binding peptides (SBPs)
  • linker-protein G (LPG)
  • surface plasmon resonance (SPR)
  • quartz crystal microbalance with dissipation monitoring (QCM-D)
  • circular dichroism (CD) spectrometry
  • equilibrium dissociation constant (KD)

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