Insights into the structure and molecular topography of the fatty acylated domain of synaptotagmin-1 |
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| Institution: | 1. Department of Medicine, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA;2. Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, CA, USA;3. Brain Research Institute, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA;4. The Pasarow Mass Spectrometry Laboratory, The Jane and Terry Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, UCLA, USA;5. Department of Molecular and Medical Pharmacology, David Geffen School of Medicine, UCLA, Los Angeles, CA, USA |
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| Abstract: | 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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