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Oral Qual: "Oligomerization of Amyloid Beta -Protein in Crowded Environments"
Start Date: 5/20/2013Start Time: 1:30 PM
End Date: 5/20/2013End Time: 2:30 PM
Event Description

Graduate Student: Matthew Voelker

Abstract: Alzheimer's Disease is strongly associated with small oligomeric assemblies formed by amyloid b-protein (ABeta), in particular with the 42 amino acids-long ABeta1-42. Recently, ABeta1-42 oligomer structure has been characterized computationally by discrete molecular dynamics (DMD) combined with implicit-solvent intermediate-resolution protein model. In vivo, ABeta1-42 coexists with other proteins and biomolecules in a crowded environment. To understand the effects of crowding on ABeta1-42 assembly, we simulated ABeta1-42 oligomer formation in the presence of crowders using the DMD approach described above. Analysis of the resulting conformations yielded an increased number of lower-order oligomers for simulations containing crowders. The monomers, tetramers, pentamers, and hexamers we observed in the presence of crowders had more Beta-strands at the N-terminus and in the central region. These conformations also had an increase in the number of contacts between the C-terminus and central region, implying more compact monomers and oligomers. Monomers with crowders also had a notably larger number of contacts between the N-terminus and C-terminus. The increased content of Beta-strands and more compact monomers and oligomers we observed are in agreement with current theoretical predictions and experimental results regarding the effects of crowding upon protein assembly.

 Advisor: Dr. Brigita Urbanc

Contact Information:
Name: Matthew Voelker
Phone: (215) 895-2732
Email: matthew.j.voelker@drexel.edu
MV
Location:
Disque Hall Room 919
Audience:
  • Current Students
  • Faculty

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