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Residue-specific structures and membrane locations of pH-low insertion peptide by solid-state nuclear magnetic resonance

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  • Nicolas S. Shu

    (State University of New York)

  • Michael S. Chung

    (State University of New York)

  • Lan Yao

    (Applied Physics and Astronomy, State University of New York)

  • Ming An

    (State University of New York)

  • Wei Qiang

    (State University of New York)

Abstract

The pH-low insertion peptide (pHLIP) binds to a membrane at pH 7.4 unstructured but folds across the bilayer as a transmembrane helix at pH∼6. Despite their promising applications as imaging probes and drug carriers that target cancer cells for cytoplasmic cargo delivery, the mechanism of pH modulation on pHLIP-membrane interactions has not been completely understood. Here, we show the first study on membrane-associated pHLIP using solid-state NMR spectroscopy. Data on residue-specific conformation and membrane location describe pHLIP in various surface-bound and membrane-inserted states at pH 7.4, 6.4 and 5.3. The critical membrane-adsorbed state is more complex than previously envisioned. At pH 6.4, for the major unstructured population, the peptide sinks deeper into the membrane in a state II′ that is distinct from the adsorbed state II observed at pH 7.4, which may enable pHLIP to sense slight change in acidity even before insertion.

Suggested Citation

  • Nicolas S. Shu & Michael S. Chung & Lan Yao & Ming An & Wei Qiang, 2015. "Residue-specific structures and membrane locations of pH-low insertion peptide by solid-state nuclear magnetic resonance," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8787
    DOI: 10.1038/ncomms8787
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