Abstract
Intracellular lipid traffic between organelles occurs primarily through a non-vesicular pathway via lipid transport proteins (LTPs). The oxysterol-binding homologue (Osh) proteins in the yeast Saccharomyces cerevisiae play an important role in the transportation of signaling lipids and are examples of LTPs. At its N-terminus, the Osh4 protein has an amphipathic lipid-packing sensor (ALPS)-like motif. To understand the kinetics of the binding of the ALPS peptide, we utilized isothermal titration calorimetry, which showed the ALPS peptide bound to liposomes containing 75% POPC-25% POPA with a KD of 129 μM.
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