{'fraction_non_alphanumeric': 0.018627450980392157, 'fraction_numerical': 0.004901960784313725, 'mean_word_length': 5.993150684931507, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Pleckstrin homology-phospholipase C-δ1 interaction with phosphatidylinositol 4,5-bisphosphate containing supported lipid bilayers monitored in situ with dual polarization interferometry.

We have determined the kinetics and affinity of binding of PH-PLCδ(1) to the PIP(2) headgroup lipids using an optical surface-sensitive technique in a time-resolved manner. The use of dual polarization interferometry to probe supported lipid bilayers (SLBs) of different compositions allowed determination of accurate affinity constants and a layer structure of the peptide binding to the model membrane platform. In addition, the platform enabled us to monitor the detailed adsorption kinetics characterized by a strong initial electrostatic attraction of the peptide to the SLB surface followed by rearrangement and loss of possibly clustered peptides upon specific binding to the phosphoinositide headgroup. These kinetics differed substantially from adsorption kinetics for nonspecific binding to similarly charged control SLBs.