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New desorption strategies for the mass spectrometric analysis of macromolecules
Author(s) -
Hutchens T. William,
Yip TaiTung
Publication year - 1993
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290070703
Subject(s) - chemistry , desorption , macromolecule , analyte , mass spectrometry , adsorption , analytical chemistry (journal) , selectivity , chromatography , nanotechnology , organic chemistry , biochemistry , materials science , catalysis
We present two new desorption strategies for the mass spectrometric analysis of macromolecules. These desorption strategies are based on the molecular design and construction of two general classes of sample ‘probe’ surfaces. The first class of surfaces is designed to enhance the desorption of intact macromolecules presented alone (neat) to the surface; we call this surface‐enhanced neat desorption (SEND). The availability of probe surfaces derivatized with, or composed of, multiple types and defined numbers of energy‐absorbing molecules will facilitate investigations of energy transfer and desorption/ionization mechanisms. The second class of probe surfaces is designed to enhance the desorption of specific macromolecules captured directly from unfractionated biological fluids and extracts; we call this surface‐enhanced affinity capture (SEAC). Use of these new probe surfaces as chemically defined solid‐phase reaction centers will facilitate protein discovery through molecular recognition in situ , and also macromolecular structure analysis through the sequential chemical and/or enzymatic modification of the adsorbed analyte in situ . Specific examples of laser‐assisted SEND and SEAC time‐of‐flight mass spectrometry are presented to illustrate the potential for increased selectivity, analyte detection sensitivity, and mass measurement accuracy.