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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Volatile anesthetic modulation of oligomerization equilibria in a hexameric model peptide
Giovanna Ghirlanda1, Simon A Hilcove, Ravindernath Pidikiti
1Department of Biophysics and Biochemistry, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Abstract:
To determine if occupancy of interfacial pockets in oligomeric proteins by volatile anesthetic molecules can allosterically regulate oligomerization equilibria, variants of a three-helix bundle peptide able to form higher oligomers were studied with analytical ultracentrifugation, hydrogen exchange and modeling. Halothane shifted the oligomerization equilibria towards the oligomer only in a mutation predicted to create sufficient volume in the hexameric pocket. Other mutations at this residue, predicted to create a too small or too polar pocket, were unaffected by halothane. Inhaled anesthetic modulation of oligomerization interactions is a novel and potentially generalizable biophysical basis for some anesthetic actions.
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