Capturing the interaction potential of amyloidogenic proteins.

Autor: Javid N; University of Dortmund, Department of Chemistry, Physical Chemistry I-Biophysical Chemistry, Otto-Hahn Strasse 6, D-44227 Dortmund, Germany., Vogtt K, Krywka C, Tolan M, Winter R
Jazyk: angličtina
Zdroj: Physical review letters [Phys Rev Lett] 2007 Jul 13; Vol. 99 (2), pp. 028101. Date of Electronic Publication: 2007 Jul 13.
DOI: 10.1103/PhysRevLett.99.028101
Abstrakt: Experimentally derived static structure factors obtained for the aggregation-prone protein insulin were analyzed with a statistical mechanical model based on the Derjaguin-Landau-Verwey-Overbeek potential. The data reveal that the protein self-assembles into equilibrium clusters already at low concentrations. Furthermore, striking differences regarding interaction forces between aggregation-prone proteins such as insulin in the preaggregated regime and natively stable globular proteins are found.
Databáze: MEDLINE