Membrane structure and interactions of human catestatin by multidimensional solution and solid-state NMR spectroscopy

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Masae SugawaraBurkhard Bechinger

Abstract

Catestatin is a natural peptide of higher organisms including humans, with a wide variety of biological functions involved in catecholamine inhibition, cardiovascular regulation, control of blood pressure, inflammation, and innate immunity. It is derived from the natural processing of chromogranin A, induced in the skin after injury, and produced by chromaffin cells and neutrophils. With neutrophils, the peptide enters the cell by crossing the plasma membrane where it interacts with internal targets to induce calcium influx. Therefore, we investigated the membrane interactions and structure of several catestatin-derived peptides. Whereas fluorescence dye release experiments are indicative of membrane permeabilization, multidimensional solution NMR and circular dichroism spectroscopies show that catestatin adopts alpha-helical conformations between Ser-6 and Tyr-12 in the presence of dodecylphosphocholine micelles. Furthermore, proton-decoupled (15)N solid-state NMR spectroscopy of sequences labeled with (15)N and reconstituted into oriented lipid bilayers indicates that this domain is aligned in a strongly tilted to inplanar alignment. Proton-decoupled (31)P NMR spectra of the same samples are indicative of conformational and/o...Continue Reading

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Apr 7, 2011·The Journal of Physical Chemistry. B·Jiadi XuAyyalusamy Ramamoorthy
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