No abstract

peptide to membranes that also contain the channel-forming peptide gramicidin A allowed us to observe the membrane adsorption of A1AT. The protein interacts with the channel and produces transient current interruptions. The on-rate of these events depends non-linearly on the A1AT concentration and scales with the mole percentage of the charged lipid in the membrane. The measured off-rate is surface-charge independent. Thus, our results suggest that the membrane lipid composition plays an important regulatory role in the physiological activity of the A1AT and its interaction with the membrane.