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Clustering and cross-linking of the wheat storage protein α-gliadin : A combined experimental and theoretical approach

Markgren, Joel LU ; Rasheed, Faiza ; Hedenqvist, Mikael S. ; Skepö, Marie LU and Johansson, Eva (2022) In International Journal of Biological Macromolecules 211. p.592-615
Abstract

Our aim was to understand mechanisms for clustering and cross-linking of gliadins, a wheat seed storage protein type, monomeric in native state, but incorporated in network while processed. The mechanisms were studied utilizing spectroscopy and high-performance liquid chromatography on a gliadin-rich fraction, in vitro produced α-gliadins, and synthetic gliadin peptides, and by coarse-grained modelling, Monte Carlo simulations and prediction algorithms. In solution, gliadins with α-helix structures (dip at 205 nm in CD) were primarily present as monomeric molecules and clusters of gliadins (peaks at 650- and 700-s on SE-HPLC). At drying, large polymers (Rg 90.3 nm by DLS) were formed and β-sheets increased (14% by FTIR).... (More)

Our aim was to understand mechanisms for clustering and cross-linking of gliadins, a wheat seed storage protein type, monomeric in native state, but incorporated in network while processed. The mechanisms were studied utilizing spectroscopy and high-performance liquid chromatography on a gliadin-rich fraction, in vitro produced α-gliadins, and synthetic gliadin peptides, and by coarse-grained modelling, Monte Carlo simulations and prediction algorithms. In solution, gliadins with α-helix structures (dip at 205 nm in CD) were primarily present as monomeric molecules and clusters of gliadins (peaks at 650- and 700-s on SE-HPLC). At drying, large polymers (Rg 90.3 nm by DLS) were formed and β-sheets increased (14% by FTIR). Trained algorithms predicted aggregation areas at amino acids 115–140, 150–179, and 250–268, and induction of liquid-liquid phase separation at P- and Poly-Q-sequences (Score = 1). Simulations showed that gliadins formed polymers by tail-to-tail or a hydrophobic core (Kratky plots and Ree = 35 and 60 for C- and N-terminal). Thus, the N-terminal formed clusters while the C-terminal formed aggregates by disulphide and lanthionine bonds, with favoured hydrophobic clustering of similar/exact peptide sections (synthetic peptide mixtures on SE-HPLC). Mechanisms of clustering and cross-linking of the gliadins presented here, contribute ability to tailor processing results, using these proteins.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Disulphide bonds, Monte Carlo simulations, Polymers, Synthetic peptides
in
International Journal of Biological Macromolecules
volume
211
pages
24 pages
publisher
Elsevier
external identifiers
  • pmid:35577195
  • scopus:85130808839
ISSN
0141-8130
DOI
10.1016/j.ijbiomac.2022.05.032
language
English
LU publication?
yes
id
de2705c2-4087-4ce8-b152-2b0b9a0b2119
date added to LUP
2022-08-24 13:02:24
date last changed
2024-11-11 05:11:33
@article{de2705c2-4087-4ce8-b152-2b0b9a0b2119,
  abstract     = {{<p>Our aim was to understand mechanisms for clustering and cross-linking of gliadins, a wheat seed storage protein type, monomeric in native state, but incorporated in network while processed. The mechanisms were studied utilizing spectroscopy and high-performance liquid chromatography on a gliadin-rich fraction, in vitro produced α-gliadins, and synthetic gliadin peptides, and by coarse-grained modelling, Monte Carlo simulations and prediction algorithms. In solution, gliadins with α-helix structures (dip at 205 nm in CD) were primarily present as monomeric molecules and clusters of gliadins (peaks at 650- and 700-s on SE-HPLC). At drying, large polymers (R<sub>g</sub> 90.3 nm by DLS) were formed and β-sheets increased (14% by FTIR). Trained algorithms predicted aggregation areas at amino acids 115–140, 150–179, and 250–268, and induction of liquid-liquid phase separation at P- and Poly-Q-sequences (Score = 1). Simulations showed that gliadins formed polymers by tail-to-tail or a hydrophobic core (Kratky plots and R<sub>ee</sub> = 35 and 60 for C- and N-terminal). Thus, the N-terminal formed clusters while the C-terminal formed aggregates by disulphide and lanthionine bonds, with favoured hydrophobic clustering of similar/exact peptide sections (synthetic peptide mixtures on SE-HPLC). Mechanisms of clustering and cross-linking of the gliadins presented here, contribute ability to tailor processing results, using these proteins.</p>}},
  author       = {{Markgren, Joel and Rasheed, Faiza and Hedenqvist, Mikael S. and Skepö, Marie and Johansson, Eva}},
  issn         = {{0141-8130}},
  keywords     = {{Disulphide bonds; Monte Carlo simulations; Polymers; Synthetic peptides}},
  language     = {{eng}},
  pages        = {{592--615}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Biological Macromolecules}},
  title        = {{Clustering and cross-linking of the wheat storage protein α-gliadin : A combined experimental and theoretical approach}},
  url          = {{http://dx.doi.org/10.1016/j.ijbiomac.2022.05.032}},
  doi          = {{10.1016/j.ijbiomac.2022.05.032}},
  volume       = {{211}},
  year         = {{2022}},
}