Elisa Cooper

Elisa Cooper

Department of Chemistry and Biochemistry

University of California, Santa Cruz

Santa Cruz, California 95064

(831) 459-2915

Fink Lab Group (from left): Dong-Pyo Hong, Elisa Cooper, Diego Sotelo, Erin Tembrina, Suzsanna Lakos, Yuki Hayashi, Nika Boder, Zhi-jie Qin, Julia Primak, Xiaoyun Meng, Wenbo Zhou, Dongmei Hu, Tony Fink

PhD, Chemistry (concentration in Biochemistry) expected Summer 2005, UC Santa Cruz

I am currently seeking a postdoctoral opportunity beginning at the end of summer or early fall 2005. View my CV

Research Interests Summary:

The molecular basis of disease
protein-protein interactions
protein folding/misfolding and degradation processes
protein structure/function relationship
new developments in biophysical methods to study protein interactions and conformation

Research:

All current projects involve the protein a-synuclein which is involved in Parkinson's disease. The ordered aggregation of a-synuclein leads to the formation of amyloid fibrils in the brains of patients with Parkinson's disease

a-synuclein Oligomerization:

Naturally occurring (transient) oligomers: Experimental evidence suggests that a-synuclein fibrillates via a nucleation dependent mechanism. However, the identity of this nucleous or 'seed' has mostly escaped examination. Also, a-synuclein has been observed to form a large variety of oligomers some believed to be 'on-pathway' intermediates to fibrillation and others thought to be 'off-pathway'. Here, the formation of a-synuclein oligomers ans the dynamics between the various oligomers have been studied through SEC-MALS experiments as well as dynamic light scattering, AFM, EM and other biophysical methods.
Stabilized oligomers: Also, under investigation are oligomers observed to form primarily due to modification of a-synuclein by external agents. Most of these oligomers are of interest because they do not go on to form fibrils.
a-synuclein A140C mutant: This mutant allows for the formation of a covalent dimer stabilized by a disulfide bond at the C-terminal amino acid. This mutant is being use to investigate the importance of dimer formation in the a-synuclein fibrillation process.

Molecular Crowding: The term molecular crowding refers to the fact that within cells a significant volume is occupied by molecules. These molecules (proteins, RNA, sugars and others) are said to provide a crowded environment for any molecule of interest. This crowding can drastically alter the kinetics or biophysical properties molecules. Here, we have applied molecular crowding theory to the problem of a-synuclein fibrillation. Artificially crowded solutions were created through the use of artificial molecular crowding agents (PEGs, Ficolls and Dextrans). Various biophysical techniques including fluorescence, CD, EM, light scattering and others have been used to study a-synuclein under crowding conditions.

Fluorescent Labeling of a-synuclein

Effects of Fe and Al on a-synuclein fibrillation

Publications:

Uversky, V.N.; Cooper, E.M.; Bower, K.S.; Li, J.; Fink, A.L. 2001. Accelerated a-synuclein fibrillation in crowded milieu. FEBS Letters 515, 99-103.

Munishkina, L.A.; Cooper, E.M.; Uversky, V.N.; Fink, A.L. 2004 The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 17, 456-464.

Cooper, E.M.; Hjülberg, D.; Villa, J.; Andrews, J.C.; DeWitt, J.G. 1997. Changes in Nickel and Lead Speciation Upon Accumulation by Metal Tolerant Datura innoxia Plant Tissue Culture. SSRL Activity Report.

Cooper, E.M.; Fink, A.L. SEC-MALS studies of a-synuclein oligomerization. In preparation.

Cooper, E.M.; Hayashi, Y.; Kalira, V.; Uversky, V.N.; Fink, A.L. The Effect of Macromolecular Crowding Agents on the Fibrillation and Biophysical Characteristics of α-Synuclein. In preparation.

Cooper, E.M.; Ahmed, A.; Fink, A.L. Is dimer formation a rate limiting step in a-synuclein fibrillation?: use of a disulfide linked a-synuclein mutant. In preparation.

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