Research Assistant Professor, Department of Biomedical Sciences
Contact Information
Email:Biosketch
Lindsey M Gottler, PhD, is the Chief Scientific Officer at Proteos, Inc, of Kalamazoo, Michigan, which is housed in the Innovation Center. She has been with Proteos, Inc, since 2008. Prior to her promotion to CSO in 2018, Dr. Gottler was a scientist and later Director of the protein purification group. Prior to joining Proteos, Dr. Gottler completed a post-doctoral fellowship at the University of Michigan in Biophysical Chemistry where she performed biophysical characterization of amyloidogenic peptides including amyloid beta and SEVI peptide. Dr. Gottler received her PhD in chemistry from the University of Michigan. Her studies included design of recombinant protein constructs for assembling non-natural, high order protein structures and study of synthetic peptides, both de novo designed and naturally occurring antimicrobial peptides, to evaluate the effects of non-natural, fluorous amino acids on protein stability, structure and function.
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Education and Training
- PhD 2008, Chemical Biology, University of Michigan-Ann Arbor
- Postdoctoral Fellowship 2008, Biophysics, University of Michigan-Ann Arbor
- BA 2002, Chemistry, Kalamazoo College
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Research
- recombinant protein purification
- recombinant protein production
- recombinant protein expression
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Publications
Polinski N.K., Volpicelli-Daley L.A., Sortwell C.E., Luk K.C., Cremades N., Gottler L.M., Froula J., Duffy M.F., Lee V.M.Y., Martinez T.N., Dave K.D. Best practices for generating and using alpha-synuclein pre-formed fibrils to model Parkinson's disease in rodents Journal of Parkinson's Disease. 2018;8(2):303-322.
Brender J.R., Hartman K., Gottler L.M., Cavitt M.E., Youngstrom D., Ramamoorthy A. Helical conformation of the SEVI precursor peptide PAP<inf>248-286</inf>, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusion Biophysical Journal. 2009;97(9):2474-2483.
Gottler L.M., Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan - A highly potent antimicrobial peptide designed from magainin Biochimica et Biophysica Acta - Biomembranes. 2009;1788(8):1680-1686.
Gottler L., Lee H., Shelburne C., Ramamoorthy A., Marsh E. Using fluorous amino acids to modulate the biological activity of an antimicrobial peptide ChemBioChem. 2008;9(3):370-373.
Gottler L.M., Bea R.D.L.S., Shelburne C.E., Ramamoorthy A., Marsh E.N.G. Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the β-hairpin antimicrobial peptide protegrin-1 Biochemistry. 2008;47(35):9243-9250.
Gottler L.M., De La Salud-Bea R., Marsh E.N.G. The fluorous effect in proteins: Properties of α<inf>4</inf>F <inf>6</inf>, a 4-α-helix bundle protein with a fluorocarbon core Biochemistry. 2008;47(15):4484-4490.