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Elucidating the Binding Mechanism of a Novel Silica-Binding Peptide.


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.

SUBMITTER: Bansal R 

PROVIDER: S-EPMC7022404 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Elucidating the Binding Mechanism of a Novel Silica-Binding Peptide.

Bansal Rachit R   Elgundi Zehra Z   Care Andrew A   C Goodchild Sophia S   S Lord Megan M   Rodger Alison A   Sunna Anwar A  

Biomolecules 20191218 1


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 <i>Streptococcus</i> 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 (<i>K</i><sub>D</sub> = 34.77 ± 11.8 nM), with a verti  ...[more]

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