Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

  • Charles H. Chen, King's College London
  • ,
  • Marcelo CR Melo, University of Pennsylvania
  • ,
  • Nils Berglund
  • Ayesha Khan, University of Exeter
  • ,
  • César de la Fuente, University of Pennsylvania
  • ,
  • Jakob P. Ulmschneider, Shanghai Jiaotong University
  • ,
  • Martin B. Ulmschneider, King's College London

Atomic detail simulations are starting to reveal how flexible polypeptides interact with fluid lipid bilayers. These insights are transforming our understanding of one of the fundamental processes in biology: membrane protein folding and assembly. Advanced molecular dynamics (MD) simulation techniques enable accurate prediction of protein structure, folding pathways and assembly in microsecond-timescales. Such simulations show how membrane-active peptides self-assemble in cell membranes, revealing their binding, folding, insertion, and aggregation, while at the same time providing atomic resolution details of peptide–lipid interactions. Essential to the impact of simulations are experimental approaches that enable calibration and validation of the computational models and techniques. In this review, we summarize the current development of applying unbiased atomic detail MD simulations and the relation to experimental techniques, to study peptide folding and provide our perspective of the field.

Original languageEnglish
JournalCurrent Opinion in Structural Biology
Volume61
Pages (from-to)160-166
Number of pages7
ISSN0959-440X
DOIs
Publication statusPublished - Apr 2020

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