The Effect of Oligomerization on A Solid-Binding Peptide Binding to Silica-Based Materials.

Bansal, R; Elgundi, Z; Goodchild, SC; Care, A; Lord, MS; Rodger, A; Sunna, A

The Effect of Oligomerization on A Solid-Binding Peptide Binding to Silica-Based Materials.

Bansal, R Elgundi, Z Goodchild, SC Care, A

Lord, MS Rodger, A Sunna, A

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Publisher:: MDPI
Publication Type:: Journal Article
Citation:: Nanomaterials (Basel, Switzerland), 2020, 10, (6)
Issue Date:: 2020-05-30

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Field	Value	Language
dc.contributor.author	Bansal, R
dc.contributor.author	Elgundi, Z
dc.contributor.author	Goodchild, SC
dc.contributor.author	Care, A https://orcid.org/0000-0002-0035-7961
dc.contributor.author	Lord, MS
dc.contributor.author	Rodger, A
dc.contributor.author	Sunna, A
dc.date.accessioned	2021-01-19T04:15:49Z
dc.date.available	2020-05-12
dc.date.available	2021-01-19T04:15:49Z
dc.date.issued	2020-05-30
dc.identifier.citation	Nanomaterials (Basel, Switzerland), 2020, 10, (6)
dc.identifier.issn	2079-4991
dc.identifier.issn	2079-4991
dc.identifier.uri	http://hdl.handle.net/10453/145486
dc.description.abstract	The bifunctional linker-protein G (LPG) fusion protein comprises a peptide (linker) sequence and a truncated form of Streptococcus strain G148 protein G (protein G). The linker represents a multimeric solid-binding peptide (SBP) comprising 4 × 21-amino acid sequence repeats that display high binding affinity towards silica-based materials. In this study, several truncated derivatives were investigated to determine the effect of the SBP oligomerization on the silica binding function of LPG (for the sake of clarity, LPG will be referred from here on as 4 × LPG). Various biophysical characterization techniques were used to quantify and compare the truncated derivatives against 4 × LPG and protein G without linker (PG). The derivative containing two sequence repeats (2 × LPG) showed minimal binding to silica, while the truncated derivative with only a single sequence (1 × LPG) displayed no binding. The derivative containing three sequence repeats (3 × LPG) was able to bind to silica with a binding affinity of KD = 53.23 ± 4.5 nM, which is 1.5 times lower than that obtained for 4 × LPG under similar experimental conditions. Circular dichroism (CD) spectroscopy and fluorescence spectroscopy studies indicated that the SBP degree of oligomerization has only a small effect on the secondary structure (the linker unravels the beginning of the protein G sequence) and chemical stability of the parent protein G. However, based on quartz crystal microbalance with dissipation monitoring (QCM-D), oligomerization is an important parameter for a strong and stable binding to silica. The replacement of three sequence repeats by a (GGGGS)12 glycine-rich spacer indicated that the overall length rather than the SBP oligomerization mediated the effective binding to silica.
dc.format	Electronic
dc.language	eng
dc.publisher	MDPI
dc.relation.ispartof	Nanomaterials (Basel, Switzerland)
dc.relation.isbasedon	10.3390/nano10061070
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	0912 Materials Engineering, 1007 Nanotechnology
dc.title	The Effect of Oligomerization on A Solid-Binding Peptide Binding to Silica-Based Materials.
dc.type	Journal Article
utslib.citation.volume	10
utslib.location.activity	Switzerland
utslib.for	0912 Materials Engineering
utslib.for	1007 Nanotechnology
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	open_access	*
pubs.consider-herdc	false
dc.date.updated	2021-01-19T04:15:05Z
pubs.issue	6
pubs.publication-status	Published
pubs.volume	10
utslib.citation.issue	6

Abstract:

The bifunctional linker-protein G (LPG) fusion protein comprises a peptide (linker) sequence and a truncated form of Streptococcus strain G148 protein G (protein G). The linker represents a multimeric solid-binding peptide (SBP) comprising 4 × 21-amino acid sequence repeats that display high binding affinity towards silica-based materials. In this study, several truncated derivatives were investigated to determine the effect of the SBP oligomerization on the silica binding function of LPG (for the sake of clarity, LPG will be referred from here on as 4 × LPG). Various biophysical characterization techniques were used to quantify and compare the truncated derivatives against 4 × LPG and protein G without linker (PG). The derivative containing two sequence repeats (2 × LPG) showed minimal binding to silica, while the truncated derivative with only a single sequence (1 × LPG) displayed no binding. The derivative containing three sequence repeats (3 × LPG) was able to bind to silica with a binding affinity of KD = 53.23 ± 4.5 nM, which is 1.5 times lower than that obtained for 4 × LPG under similar experimental conditions. Circular dichroism (CD) spectroscopy and fluorescence spectroscopy studies indicated that the SBP degree of oligomerization has only a small effect on the secondary structure (the linker unravels the beginning of the protein G sequence) and chemical stability of the parent protein G. However, based on quartz crystal microbalance with dissipation monitoring (QCM-D), oligomerization is an important parameter for a strong and stable binding to silica. The replacement of three sequence repeats by a (GGGGS)12 glycine-rich spacer indicated that the overall length rather than the SBP oligomerization mediated the effective binding to silica.

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http://hdl.handle.net/10453/145486