title: Orientational alignment of amyloidogenic proteins in pre-aggregated solutions.
abstract: In the present study we combine dielectric relaxation spectroscopy with generalized Born simulations to explore the role of orientational order for protein aggregation in solutions of bovine pancreatic insulin at various pH conditions. Under aggregation-prone conditions at low pH, insulin monomers prefer antiparallel dipole alignments, which are consistent with the orientation of the monomeric subunits in the dimer structure. This alignment is also true for two dimers, suggesting that already at moderate protein concentrations the species assemble in equilibrium clusters, in which the molecules adopt preferred orientations also found for the protomers of the corresponding oligomers.
authors: Department of Computational Biological Chemistry, University of Vienna, Währingerstrasse 17, 1090 Vienna, Austria.
authors: C
authors: C
authors: Schröder
authors: Department of Computational Biological Chemistry, University of Vienna, Währingerstrasse 17, 1090 Vienna, Austria.
authors: O
authors: O
authors: Steinhauser
authors: Department of Physical Chemistry II, Ruhr-University of Bochum, Germany and Praj Matrix The Innovation Center Urawade, Pune 412108, India.
authors: P
authors: P
authors: Sasisanker
authors: Department of Physical Chemistry II, Ruhr-University of Bochum, Building NC 6-25, 44780 Bochum, Germany.
authors: H
authors: H
authors: Weingärtner
mesh_terms: D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D002417:Cattle; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D066329:Protein Aggregates; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D012996:Solutions
chemical_list: D058227:Amyloidogenic Proteins; D007328:Insulin; D066329:Protein Aggregates; D012996:Solutions