Christian Bleiholder

Christian Bleiholder

Tel: 805-893-2673


I obtained my M.Sc. in 2004 at the University of Heidelberg in the laboratory of Prof. R. Gleiter (Institute of Organic Chemistry) and my Ph.D. in 2007 at the German Cancer Research Center (Profs. R. Gleiter and S. Suhai, Department of Molecular Biophysics). Subsequently, I joined the laboratory of Prof. Bowers at UCSB in 2008 to pursue postdoctoral studies in ion mobility spectrometry-mass spectrometry (IMS-MS). My awards include an Alexander-von-Humboldt Fellowship (2007) and a Postdoctoral Research Award of the American Chemical Society (2011).

My research in the Bowers group focuses on the formation of fibrillar protein assemblies implicated in amyloid diseases, including Alzheimer’s and type 2 diabetes. Understanding the fundamental principles that relate aggregation, morphology and biochemistry of soluble peptide aggregates is central to developing diagnostic and therapeutic strategies for amyloid diseases. So far, these processes have resisted detailed characterization due to the transient and dynamic nature of early peptide oligomers. Our recently published results (Nature Chemistry, 2011) show transitions of early, soluble peptide oligomers from a globular to a fibrillar conformation, demonstrating that IMS-MS is capable of elucidating the structural processes involved during the onset of amyloid formation.

The theory of ion mobility is another aspect of my research with Prof. Bowers. One of the crucial unsolved problems in ion mobility studies is the efficient and accurate determination of collision cross sections of macromolecular species from model structures, especially for biological macromolecules. Good algorithms exist for small systems but once the molecule reaches several thousand atoms the projection methods become unacceptably inaccurate and the trajectory method becomes unacceptably time consuming. This, and larger, are size regimes that many are now working in. Recently (IJMS, in press), we presented a modified version of the projection method that retains much of is computational efficiency while adding the accuracy of the trajectory method. The software implementation will be made publicly available.

Previous work involved quantum mechanical modeling of transition metal complexes, intermolecular interactions, as well as the gas-phase chemistry of protonated peptides.