Peptoids are complex and diverse oligomeric structures which have been explored for a number of applications including drug molecules, surfactants of catalysts.
1-2 In contrast to their amino-acid composed peptide counterparts they are highly flexible and diverse, spanning a large design space of chemical and structural functionality through the careful tuning of their side chains. One novel example of this is the N-substituted α-chiral, aromatic side chains oligomers which can produce stable helical structures in both aqueous and non-aqueous solutions.
3 These oligomers have been shown to have the capacity to assemble into more complex hierarchical assemblies like microspheres, nanosheets, and dynamic single-walled nanotube structures.
4 However, little is known about the mechanisms of these assemblies. Molecular dynamics provide an opportunity to understand this dynamic behavior at an atomistic-level of detail. Here we present our extension of the MFTOID peptoid forcefield
5 to investigate the mechanisms that give rise to these unique complex assemblies.
[1] Dohm MT, Kapoor R, Barron AE. Peptoids: Bio-Inspired Polymers as Potential Pharmaceuticals. Curr. Pharm. 2011, 47 (17), 2732
[2] Maayan G, Ward MD, Kirshenbaum K. Folded biomimetic oligomers for enantioselective catalysis. Proc Natl Acad Sci 2019, 106(33):13679-84
[3] Wu C, Sanborn S, Huang K, Zuckermann RN, Barron AE. Peptoid Oligomers with α-Chiral, Aromatic Side Chains: Sequence Requirements for the Formation of Stable Peptoid Helices. J. Am. Chem. Soc. 2001, 123, 28, 6778-6784
[4] Weiser LJ, Santiso EE, Molecular modeling studies of peptoid polymers. AIMS Materials Science, 2017 4(5): 1029-1051.
[5] Mirijanian DT, Mannige RV, Zuckermann RN, et al. Development and use of an atomistic CHARMM-based forcefield for peptoid simulation. J Comput Chem. 2014. 35: 360–370
