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• W2018127651 abstract "Abstract 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." @default.
• W2018127651 created "2016-06-24" @default.
• W2018127651 creator A5041072805 @default.
• W2018127651 creator A5048922511 @default.
• W2018127651 date "2012-07-13" @default.
• W2018127651 modified "2023-10-18" @default.
• W2018127651 title "Structure-Directing<scp>L</scp>-Tryptophan for Supported DPPC Helices and Fractals: An Alkyl-Chain Tilt-Angle Dependence" @default.
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• W2018127651 doi "https://doi.org/10.1002/cplu.201200075" @default.
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