pH-dependent thermodynamic intermediates of pHLIP membrane insertion determined by solid-state NMR spectroscopy.
Related Articles pH-dependent thermodynamic intermediates of pHLIP membrane insertion determined by solid-state NMR spectroscopy.
Proc Natl Acad Sci U S A. 2018 11 27;115(48):12194-12199
Authors: Otieno SA, Hanz SZ, Chakravorty B, Zhang A, Klees LM, An M, Qiang W
Abstract
The applications of the pH low insertion peptide (pHLIP) in cancer diagnosis and cross-membrane cargo delivery have drawn increasing attention in the past decade. With its origin as the transmembrane (TM) helix C of bacteriorhodopsin, pHLIP is also an important model for understanding how pH can affect the folding and topogenesis of a TM ?-helix. Protonations of multiple D/E residues transform pHLIP from an unstructured coil at membrane surface (known as state II, at pH >= 7) to a TM ?-helix (state III, pH