Journal
CHEMPLUSCHEM
Volume 77, Issue 10, Pages 898-907Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cplu.201200075
Keywords
helical structures; molecular dynamics; molecular tilt angle; polarised FT-IRRAS; trans-membrane tryptophan
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Funding
- Department of Science and Technology, New Delhi, India [SR/S2/CMP-57/2006]
- IIT Madras
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This study reports supported one-dimensional fractals and helices of dipalmitoylphosphatidylcholine (DPPC) from interfacial and trans-membrane L-tryptophan interactions. One of the key challenges in the fabrication of phospholipid helices is unravelled using simple 2D nanotechnology techniques and the amphipathic membrane-exposed amino acid L-tryptophan. Unlike in earlier reports, in which self-assembly induced helicity exclusively to the peptide backbone in a lipid environment, this study infers the amino acid to govern the assembly of anisotropic, large-curvature lipid helices through diverse interactions such as insertion, folding, dipole reorientation, steric interactions and molecular tilt dependence, culminating in the induction of helicity in a nonhelical lipid. Molecular dynamics simulations succinctly corroborate the helix formation, implying that trans-membrane tryptophans support such segmental interactions.
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