Synthesis and protein binding studies of a peptide fragment of clathrin assembly protein AP180 bearing an O-linked -N-acetylglucosaminyl-6-phosphate modificationElectronic supplementary information (ESI) available: 1H and 13C NMR spectra of novel compounds and characterisation of peptide 1, glycopeptide 2 and glycophosphopeptide 3. See DOI: 10.1039/c2ob07139h

A novel post-translational modification of threonine, - N -acetylglucosaminyl-phosphate, was recently discovered on assembly protein AP180, a protein which plays a crucial role in clathrin coated vesicle formation in synaptic vesicle endocytosis (SVE). Herein, we report studies aimed at probing the effect of this modification on binding to proteins in rat brain lysate using pull down experiments with peptide fragments of AP180. The synthesis and protein binding studies of a peptide fragment of AP180 bearing a recently discovered post-translational modification of threonine, - N -acetylglucosaminyl-phosphate, is described.