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

doi:10.3390/biom10010004

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

ARC Centre of Excellence for Nanoscale BioPhotonics (CNBP)

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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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 (K_D = 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 language	English
Article number	4
Pages (from-to)	1-15
Number of pages	15
Journal	Biomolecules
Volume	10
Issue number	1
DOIs	https://doi.org/10.3390/biom10010004
Publication status	Published - Jan 2020

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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10.3390/biom10010004

Publisher version (open access)Final published version, 1.57 MBLicence: CC BY

Cite this

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title = "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.",

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author = "Rachit Bansal and Zehra Elgundi and Andrew Care and Goodchild, {Sophia C.} and Lord, {Megan S.} and Alison Rodger and Anwar Sunna",

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. ",

year = "2020",

month = jan,

doi = "10.3390/biom10010004",

language = "English",

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T1 - Elucidating the binding mechanism of a novel silica-binding peptide

AU - Bansal, Rachit

AU - Elgundi, Zehra

AU - Care, Andrew

AU - Goodchild, Sophia C.

AU - Lord, Megan S.

AU - Rodger, Alison

AU - Sunna, Anwar

N1 - 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.

PY - 2020/1

Y1 - 2020/1

N2 - 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.

AB - 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.

KW - solid-binding peptides (SBPs)

KW - linker-protein G (LPG)

KW - surface plasmon resonance (SPR)

KW - quartz crystal microbalance with dissipation monitoring (QCM-D)

KW - circular dichroism (CD) spectrometry

KW - equilibrium dissociation constant (KD)

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U2 - 10.3390/biom10010004

DO - 10.3390/biom10010004

M3 - Article

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SN - 2218-273X

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SP - 1

EP - 15

JO - Biomolecules

JF - Biomolecules

IS - 1

M1 - 4

ER -

Elucidating the binding mechanism of a novel silica-binding peptide

Abstract

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Keywords

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ARC CoE Nanoscale BioPhotonics (CNBP) (RAAP)

Cite this

Elucidating the binding mechanism of a novel silica-binding peptide

Abstract

Bibliographical note

Keywords

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Fingerprint

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ARC CoE Nanoscale BioPhotonics (CNBP) (RAAP)

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