Capturing the Interaction Potential of Amyloidogenic Proteins

Journal Article · Fri Jul 13 00:00:00 EDT 2007 · Physical Review Letters

DOI:https://doi.org/10.1103/PHYSREVLETT.99.028101· OSTI ID:20957890

Javid, Nadeem; Vogtt, Karsten; Winter, Roland ^[1]; Krywka, Christina; Tolan, Metin ^[2]

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1. University of Dortmund, Department of Chemistry, Physical Chemistry I-Biophysical Chemistry, Otto-Hahn Strasse 6, D-44227 Dortmund (Germany)
2. Physics Department/DELTA, University of Dortmund, D-44221 Dortmund (Germany)

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.

• OSTI ID: 20957890
• Journal Information: Physical Review Letters, Vol. 99, Issue 2; Other Information: DOI: 10.1103/PhysRevLett.99.028101; (c) 2007 The American Physical Society; Country of input: International Atomic Energy Agency (IAEA); ISSN 0031-9007
• Country of Publication: United States
• Language: English

Related Subjects

71 CLASSICAL AND QUANTUM MECHANICS
GENERAL PHYSICS
AGGLOMERATION
EQUILIBRIUM
INSULIN
INTERACTIONS
POTENTIALS
STRUCTURE FACTORS