Experimental and theoretical tools to elucidate the binding mechanisms of solid-binding peptides.

Bansal, R; Care, A; Lord, MS; Walsh, TR; Sunna, A

Experimental and theoretical tools to elucidate the binding mechanisms of solid-binding peptides.

Bansal, R Care, A

Lord, MS Walsh, TR Sunna, A

Permalink

Publisher:: ELSEVIER SCIENCE BV
Publication Type:: Journal Article
Citation:: N Biotechnol, 2019, 52, pp. 9-18
Issue Date:: 2019-09-25

Closed Access

	Filename	Description	Size
	1-s2.0-S1871678418319332-main.pdf		4.36 MB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Bansal, R
dc.contributor.author	Care, A https://orcid.org/0000-0002-0035-7961
dc.contributor.author	Lord, MS
dc.contributor.author	Walsh, TR
dc.contributor.author	Sunna, A
dc.date.accessioned	2022-03-25T04:20:47Z
dc.date.available	2019-04-01
dc.date.available	2022-03-25T04:20:47Z
dc.date.issued	2019-09-25
dc.identifier.citation	N Biotechnol, 2019, 52, pp. 9-18
dc.identifier.issn	1871-6784
dc.identifier.issn	1876-4347
dc.identifier.uri	http://hdl.handle.net/10453/155553
dc.description.abstract	The interactions between biomolecules and solid surfaces play an important role in designing new materials and applications which mimic nature. Recently, solid-binding peptides (SBPs) have emerged as potential molecular building blocks in nanobiotechnology. SBPs exhibit high selectivity and binding affinity towards a wide range of inorganic and organic materials. Although these peptides have been widely used in various applications, there is a need to understand the interaction mechanism between the peptide and its material substrate, which is challenging both experimentally and theoretically. This review describes the main characterisation techniques currently available to study SBP-surface interactions and their contribution to gain a better insight for designing new peptides for tailored binding.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	ELSEVIER SCIENCE BV
dc.relation	http://purl.org/au-research/grants/arc/CE140100003
dc.relation.ispartof	N Biotechnol
dc.relation.isbasedon	10.1016/j.nbt.2019.04.001
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	06 Biological Sciences, 10 Technology
dc.subject.classification	Biotechnology
dc.subject.mesh	Amino Acid Sequence
dc.subject.mesh	Biophysical Phenomena
dc.subject.mesh	Models, Molecular
dc.subject.mesh	Peptides
dc.subject.mesh	Protein Binding
dc.subject.mesh	Peptides
dc.subject.mesh	Amino Acid Sequence
dc.subject.mesh	Protein Binding
dc.subject.mesh	Models, Molecular
dc.subject.mesh	Biophysical Phenomena
dc.title	Experimental and theoretical tools to elucidate the binding mechanisms of solid-binding peptides.
dc.type	Journal Article
utslib.citation.volume	52
utslib.location.activity	Netherlands
utslib.for	06 Biological Sciences
utslib.for	10 Technology
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	closed_access	*
dc.date.updated	2022-03-25T04:20:45Z
pubs.publication-status	Published
pubs.volume	52

Abstract:

The interactions between biomolecules and solid surfaces play an important role in designing new materials and applications which mimic nature. Recently, solid-binding peptides (SBPs) have emerged as potential molecular building blocks in nanobiotechnology. SBPs exhibit high selectivity and binding affinity towards a wide range of inorganic and organic materials. Although these peptides have been widely used in various applications, there is a need to understand the interaction mechanism between the peptide and its material substrate, which is challenging both experimentally and theoretically. This review describes the main characterisation techniques currently available to study SBP-surface interactions and their contribution to gain a better insight for designing new peptides for tailored binding.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/155553