Self-assembly and hydrogelation of a potential bioactive peptide derived from quinoa proteins

Simple item page
dc.citation.issuePt 2
dc.citation.volume259
dc.contributor.authorCheng L
dc.contributor.authorDe Leon-Rodriguez L
dc.contributor.authorGilbert EP
dc.contributor.authorLoo T
dc.contributor.authorPetters L
dc.contributor.authorYang Z
dc.coverage.spatialNetherlands
dc.date.accessioned2024-04-30T02:40:23Z
dc.date.accessioned2024-07-25T06:50:04Z
dc.date.available2024-01-09
dc.date.available2024-04-30T02:40:23Z
dc.date.available2024-07-25T06:50:04Z
dc.date.issued2024-02
dc.description.abstractIn this work the identification of peptides derived from quinoa proteins which could potentially self-assemble, and form hydrogels was carried out with TANGO, a statistical mechanical based algorithm that predicts β-aggregate propensity of peptides. Peptides with the highest aggregate propensity were subjected to gelling screening experiments from which the most promising bioactive peptide with sequence KIVLDSDDPLFGGF was selected. The self-assembling and hydrogelation properties of the C-terminal amidated peptide (KIVLDSDDPLFGGF-NH2) were studied. The effect of concentration, pH, and temperature on the secondary structure of the peptide were probed by circular dichroism (CD), while its nanostructure was studied by transmission electron microscopy (TEM) and small-angle neutron scattering (SANS). Results revealed the existence of random coil, α-helix, twisted β-sheet, and well-defined β-sheet secondary structures, with a range of nanostructures including elongated fibrils and bundles, whose proportion was dependant on the peptide concentration, pH, or temperature. The self-assembly of the peptide is demonstrated to follow established models of amyloid formation, which describe the unfolded peptide transiting from an α-helix-containing intermediate into β-sheet-rich protofibrils. The self-assembly is promoted at high concentrations, elevated temperatures, and pH values close to the peptide isoelectric point, and presumably mediated by hydrogen bond, hydrophobic and electrostatic interactions, and π-π interactions (from the F residue). At 15 mg/mL and pH 3.5, the peptide self-assembled and formed a self-supporting hydrogel exhibiting viscoelastic behaviour with G' (1 Hz) ~2300 Pa as determined by oscillatory rheology measurements. The study describes a straightforward method to monitor the self-assembly of plant protein derived peptides; further studies are needed to demonstrate the potential application of the formed hydrogels in food and biomedicine.
dc.description.confidentialfalse
dc.edition.editionFebruary 2024
dc.format.pagination129296-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/38199549
dc.identifier.citationCheng L, De Leon-Rodriguez LM, Gilbert EP, Loo T, Petters L, Yang Z. (2024). Self-assembly and hydrogelation of a potential bioactive peptide derived from quinoa proteins.. Int J Biol Macromol. 259. Pt 2. (pp. 129296-).
dc.identifier.doi10.1016/j.ijbiomac.2024.129296
dc.identifier.eissn1879-0003
dc.identifier.elements-typejournal-article
dc.identifier.issn0141-8130
dc.identifier.number129296
dc.identifier.piiS0141-8130(24)00099-0
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/70972
dc.languageeng
dc.publisherElsevier BV
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S0141813024000990
dc.relation.isPartOfInt J Biol Macromol
dc.rights(c) 2024 The Author/s
dc.rightsCC BY-NC-ND 4.0
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectFibrillar hydrogels
dc.subjectNanostructures
dc.subjectProtofibrils
dc.subjectQuinoa proteins
dc.subjectRheology
dc.subjectSecondary structures
dc.subjectSelf-assembly
dc.subjectChenopodium quinoa
dc.subjectPeptides
dc.subjectHydrogels
dc.subjectProtein Structure, Secondary
dc.subjectNanostructures
dc.subjectCircular Dichroism
dc.titleSelf-assembly and hydrogelation of a potential bioactive peptide derived from quinoa proteins
dc.typeJournal article
pubs.elements-id485525
pubs.organisational-groupOther
Files
Original bundle
Now showing 1 - 2 of 2
Thumbnail Image
Name:
485525 PDF.pdf
Size:
4.93 MB
Format:
Adobe Portable Document Format
Description:
Download
Thumbnail Image
Name:
Evidence
Size:
329.98 KB
Format:
Microsoft Word XML
Description:
Download
Collections
Journal Articles