Carl Frieden, Ph.D.

Biochemistry and Molecular Biophysics

General Program

  • 314-362-3344

  • 314-362-3342

  • 314-362-7183

  • 215 McDonnell Medical Sciences Building



  • apoE lipoproteins,, intrinsically disordered proteins, amyloid-beta, Alzheimer’s Disease, bacterial infection, curli proteins

  • Protein structure/function relationships

Research Abstract:

The project in my laboratory is the study of the apolipoprotein E (apoE) family of proteins and their relation to late-onset Alzheimer’s Disease (AD). It has been well-established that, of the three isoforms of this 34 kDa protein, which differ only by single amino acid changes, apoE4 is the major risk factor for AD while apoE3, the most common form, is not implicated in developing AD. The majority of those with AD can be correlated with the presence of at least one copy of apoE4. We study the differences between the apoE isoforms using biophysical techniques with the goal of understanding why the different apoE isoforms have different functional properties. Work will also include the interaction of apoE with amyloid-beta (Aß) and with tau, both of which are associated with Alzheimer’s disease.

Selected Publications:

Frieden, C, Wang, H. and Ho, C. M. W., A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions Proc Natl Acad Sci. (2017) 114 6292-6297 PMID: 28559318.
Wang, Hanliu, Rempel, Don, Giblin, Daryl, Frieden, Carl, Gross, Michael. Peptide-level interactions between proteins and small-molecule drug candidates by HDX-MS, PLIMSTEX and modified SUPREX: the example of ApoE3 (2017) Anal Biochem (2017) 89 10687-10695

C. Frieden. ApoE: The role of conserved residues in defining function. Prot Sci 24 138-144 (2015) PMC4282419

T. Mondal, H .Wang, G. T. DeKoster, B. Baban, M. L. Gross and C. Frieden. ApoE: In vitro studies of a small molecule effector. Biochemistry (2016) 55 2613-2621 PMCID4976638

K. Garai and C. Frieden, Quantitative analysis of the time course of A oligomerization and subsequent growth steps using tetramethylrhodamine-labeled A. Proc Natl Acad Sci (USA) 110 3321-3326 (2013) PMCID: PMCID3587211

R. Huang, K. Garai, C. Frieden and M. Gross, Interface determination and dynamics of apolipoprotein E oligomerization by hydrogen deuterium exchange and electron-transfer dissociation mass spectrometry. Biochemistry. 50 9273-9282 (2011).PMC3202646

K. Garai, B. Baban and C. Frieden. Dissociation of apoE oligomers to monomer is required for high affinity binding to phospholipid vesicles. Biochemistry. 50 2550-2558 (2011). PMC3088999

K. Garai, B. Baban and C. Frieden. Self-association and stability of the apoe isoforms at low pH: implications for apoE-lipid interactions. Biochemistry. 50 6356-6364 (2011). PMID21699199

Last Updated: 7/31/2018 7:54:10 AM

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