Dimerization of helical β-peptides in solution

Michael McGovern, Nicholas Abbott, Juan J. De Pablo

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Molecular simulations are used to examine the aggregation behavior of several β-peptides in explicit water. The particular peptides considered here adopt a helical, rodlike conformation in aqueous solution. Four distinct molecular sequences are considered. Earlier experimental studies have revealed the formation of ordered and disordered aggregates for such molecules, depending on sequence. The simulations reported here, which are conducted by resorting to metadynamics techniques, lead to free energy surfaces for dimerization of the peptides in water as a function of separation and relative orientation. Such surfaces are used to identify the molecular origins for the behaviors observed in the experiments.

Original languageEnglish (US)
Pages (from-to)1435-1442
Number of pages8
JournalBiophysical journal
Issue number6
StatePublished - Mar 21 2012

Bibliographical note

Funding Information:
This work is supported by the National Science Foundation through the Nanoscale Science and Engineering Center at the University of Wisconsin-Madison.

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