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.
(Less)
- author
- Markgren, Joel
LU
; Rasheed, Faiza
; Hedenqvist, Mikael S.
; Skepö, Marie
LU
and Johansson, Eva
- organization
- publishing date
- 2022
- 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
-
- scopus:85130808839
- pmid:35577195
- 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
- 2025-10-28 10:36:20
@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}},
}