Mass spectrometry: Metamorphosis from an analytical technique to a preparative technology
Abstract
The focus of this thesis is the ion/surface collision phenomena at hyperthermal energies, in the range of laboratory energies of 1--100 eV. It particularly emphasizes collisions of large organic ions with organic surfaces at energies corresponding to deposition of ions on surfaces without adverse effects on their structure and/or bioactivity, also known as soft-landing. An overview of the assumptions and prior work in the field of mass spectrometry is used to introduce the reader to the concept of mass spectrometry as an analytical and preparative technique for separation and purification of proteins, with or without charge neutralization upon surface deposition and with preservation bioactivity. Liquid and functionalized surfaces are discussed in the context of finding functionalized surfaces for preservation of bioactivity of soft-landed ions. New capabilities for mass spectrometry are demonstrated by showing that it is possible to soft land proteins and peptides from complex mixtures into glycerol-based liquid surfaces with preservation of bioactivity. It is also shown that appropriate liquid surfaces can be used without any additional treatment to detect the soft-landed material by electrospray ionization (ESI), electrosonic spray ionization (ESSI)[20] or matrix-assisted laser desorption ionization mass spectrometry (MALDI). The liquids can also be further processed to extract the purified protein. Importantly, by adding appropriate enzymes to the liquid surfaces used as soft-landing substrates, the nature of purified proteins can be determined through enzymatic reactions.
Degree
Ph.D.
Advisors
Cooks, Purdue University.
Subject Area
Analytical chemistry
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