Insights into the structure and molecular topography of the fatty acylated domain of synaptotagmin-1.
Biochimica et biophysica acta. Biomembranes(2019)
摘要
Abundant attention has focused on synaptotagmin's C2 domains, but less is known about the structure and function of its other regions. Here, we synthesized the N-acetylated, C-end amidated and Cys-palmitated peptide (VLTCCFCICK KCLFKKKNKK K) which includes the fatty acylated cysteine residues in the membrane-affiliated domain of synaptotagmin-1. Fourier-transform infrared spectrometry indicated that this peptide's conformation is influenced by environmental polarity. In artificial bilayer membranes, this peptide exhibited abundant β-structure. Electron microscopy revealed that this peptide also promoted the stacking of liposome membranes. Together these results suggest that the fatty acylated region of synaptotagmin-1 is likely to adopt β-structure in biological membranes. This preference for β-structure versus α-helix has functional implications for the role of synaptotagmin-1 in synaptic vesicle exocytosis.
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