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Electrospray ionization mass spectrometry of oligonucleotide complexes with drugs, metals, and proteins
Author(s) -
Beck Jennifer L.,
Colgrave Michelle L.,
Ralph Stephen F.,
Sheil Margaret M.
Publication year - 2001
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.1003
Subject(s) - chemistry , electrospray ionization , dna , non covalent interactions , mass spectrometry , covalent bond , tandem mass spectrometry , oligonucleotide , protein mass spectrometry , small molecule , top down proteomics , electrospray , molecule , combinatorial chemistry , chromatography , biochemistry , organic chemistry , hydrogen bond
I. Introduction 61 II. Binding of Small Molecules to DNA 62A. Covalent Binding 62B. Reversible (Noncovalent) DNA‐Binding Agents 65 III. DNA–Metal Ion Complexes 67A. Platinum Complexes 70B. Other Metal Ions 73 IV. DNA–Protein Complexes 74A. Introduction 74B. ESI‐MS of DNA–Protein Complexes 76C. ESI‐MS Analysis of Proteolytic Products of DNA–Protein Complexes 79D. ESI‐MS of Ternary DNA–Protein–Ligand Complexes 80 V. Conclusions 80 Abbreviations 81 References 81Interactions of DNA with drugs, metal ions, and proteins are important in a wide variety of biological processes. With the advent of electrospray ionization (ESI) and matrix‐assisted laser desorption ionization (MALDI), mass spectrometry (MS) is now a well‐established tool for the characterization of the primary structures of biopolymers. The gentle nature of the ESI process, however, means that ESI‐MS is also finding application for the study of noncovalent and other fragile biomolecular complexes. We outline here the progress, to date, in the use of ESI‐MS for the study of noncovalent drug—DNA and protein—DNA complexes together with strategies that can be employed to examine the binding of small molecules and metal complexes to DNA. In the case of covalent complexes with DNA, sequence information can be derived from ESI‐MS used in conjunction with tandem mass spectrometry (MS/MS) and/or enzymatic digestion. MS/MS can also be used to probe the relative binding affinities of drugs that bind to DNA via noncovalent interactions. Overall, the work in this area, to date has demonstrated that ESI‐MS and MS/MS will prove to be valuable complements to other structural methods, offering advantages in terms of speed, specificity, and sensitivity. © 2001 John Wiley & Sons, Inc., Mass Spec Rev 20: 61–87, 2001