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Structure-Directing L-Tryptophan for Supported DPPC Helices and Fractals: An Alkyl-Chain Tilt-Angle Dependence

Authors

  • Nirod Kumar Sarangi,

    1. Department of Chemistry, Indian Institute of Technology Madras, Chennai 600 036 (India), Fax: (+91) 44-2257-4202
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  • Prof. Archita Patnaik

    Corresponding author
    1. Department of Chemistry, Indian Institute of Technology Madras, Chennai 600 036 (India), Fax: (+91) 44-2257-4202
    • Department of Chemistry, Indian Institute of Technology Madras, Chennai 600 036 (India), Fax: (+91) 44-2257-4202
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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.

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