Atomistic modeling of peptide aggregation and β-sheet structuring in corn zein for viscoelasticity

Daniel P. Erickson, Martha Dunbar, Elham Hamed, Oguz K. Ozturk, Osvaldo H. Campanella*, Sinan Keten, Bruce R. Hamaker

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The structure−function relationships of plant-based proteins that give rise to desirable texture attributes in order to mimic meat products are generally unknown. In particular, it is not clear how to engineer viscoelasticity to impart cohesiveness and proper mouthfeel; however, it is known that intermolecular β-sheet structures have the potential to enhance the viscoelastic property. Here, we investigated the propensity of selected peptide segments within common corn α-zein variants to maintain stable aggregates and β-sheet structures. Simulations on dimer systems showed that stability was influenced by the initial orientation and the presence of contiguous small hydrophobic residues. Simulations using eight-peptide β-sheet oligomers revealed that peptide sequences without proline had higher levels of β-sheet structuring. Additionally, we identified that sequences with a dimer hydrogen-bonding density of >22% tended to have a larger percent β-sheet conformation. These results contribute to understanding how the viscoelasticity of zein can be increased for use in plant-based meat analogues.

Original languageEnglish (US)
Pages (from-to)1856-1866
Number of pages11
Issue number5
StatePublished - May 10 2021

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


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