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

Bansal, R; Elgundi, Z; Care, A; C Goodchild, S; S Lord, M; Rodger, A; Sunna, A

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

Bansal, R Elgundi, Z Care, A

C Goodchild, S S Lord, M Rodger, A Sunna, A

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Publisher:: MDPI
Publication Type:: Journal Article
Citation:: Biomolecules, 2019, 10, (1)
Issue Date:: 2019-12-18

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Field	Value	Language
dc.contributor.author	Bansal, R
dc.contributor.author	Elgundi, Z
dc.contributor.author	Care, A https://orcid.org/0000-0002-0035-7961
dc.contributor.author	C Goodchild, S
dc.contributor.author	S Lord, M
dc.contributor.author	Rodger, A
dc.contributor.author	Sunna, A
dc.date.accessioned	2022-03-25T04:17:35Z
dc.date.available	2019-12-16
dc.date.available	2022-03-25T04:17:35Z
dc.date.issued	2019-12-18
dc.identifier.citation	Biomolecules, 2019, 10, (1)
dc.identifier.issn	2218-273X
dc.identifier.issn	2218-273X
dc.identifier.uri	http://hdl.handle.net/10453/155551
dc.description.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.
dc.format	Electronic
dc.language	eng
dc.publisher	MDPI
dc.relation.ispartof	Biomolecules
dc.relation.isbasedon	10.3390/biom10010004
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	0601 Biochemistry and Cell Biology
dc.subject.mesh	Adsorption
dc.subject.mesh	Antibodies
dc.subject.mesh	Circular Dichroism
dc.subject.mesh	Kinetics
dc.subject.mesh	Peptides
dc.subject.mesh	Silicon Dioxide
dc.subject.mesh	Surface Plasmon Resonance
dc.subject.mesh	Silicon Dioxide
dc.subject.mesh	Peptides
dc.subject.mesh	Antibodies
dc.subject.mesh	Circular Dichroism
dc.subject.mesh	Surface Plasmon Resonance
dc.subject.mesh	Kinetics
dc.subject.mesh	Adsorption
dc.title	Elucidating the Binding Mechanism of a Novel Silica-Binding Peptide.
dc.type	Journal Article
utslib.citation.volume	10
utslib.location.activity	Switzerland
utslib.for	0601 Biochemistry and Cell Biology
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access	*
dc.date.updated	2022-03-25T04:17:31Z
pubs.issue	1
pubs.publication-status	Published online
pubs.volume	10
utslib.citation.issue	1

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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http://hdl.handle.net/10453/155551