FRAGMENTATION OF LIPOSOMES BY HYDROPHOBICALLY-MODIFIED POLYPEPTOIDS: ELUCIDATING THE ROLE OF MOLECULAR CHARACTERISTICS

ORAL

Abstract

Amphiphiles (e.g. membrane scaffold protein, styrene-co-maleic acid, etc.) stabilized lipid nanodiscs have been developed as water-soluble membrane mimetic platforms to stabilize membrane proteins for further structural characterizations. In contrast to detergent micelles, the structures of membrane proteins in nanodiscs are better retained with enhanced long-term stabilities.
In this work, hydrophobically modified polypeptoids (HMPs) have been designed and investigated as facially amphiphiles to fragment liposome to form stable HMP-lipid complexes or nanodiscs. The effects of polymer concentration, chain length, and relative hydrophobicity on liposome fragmentation have been elucidated by a combination of DLS, SLS and EM analysis. It was found that HMPs with relatively higher polymer hydrophobicity (De mol % = 27 %) and longer chain length (DPn =100) can induce more effective liposome fragmentation relative to short polymers (DPn = 34-60) and hydrophilic polymers with similar chain length (DPn = 96 with De mol % = 16 %). It is hypothesized that a high local hydrophobic contact between polymers and lipid membranes is critical to accelerate and enhance the extent of liposome fragmentation.

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Presenters

  • Tianyi Yu

    • Louisiana State University

Authors

  • Tianyi Yu

    • Louisiana State University

  • Marzhana Omarova

    • Department of Chemical and Biomolecular Engineering, Tulane University

  • Vijay T John

    • Department of Chemical and Biomolecular Engineering, Tulane University
    • Tulane University

  • Donghui Zhang

    • Louisiana State University