Subtle differences in molecular recognition between modified glycopeptide antibiotics and bacterial receptor peptides identified by electrospray ionization mass spectrometry

Jørgensen, Thomas J. D.; Staroske, Thomas; Roepstorff, Peter; Williams, Dudley H.; Heck, Albert J. R.

doi:10.1039/a904504j

Cited by 39 publications

(27 citation statements)

References 26 publications

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“…Speci®city and relative af®nities can be determined by a comparison of the relative intensities of ions that correspond to the complex and uncomplexed macromolecules. Caution must be exercised so that ions that arise from complexes of similar composition are compared, because these complexes will have comparable ionization ef®ciencies (Jorgensen et al, 1999).…”

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confidence: 99%

Electrospray ionization mass spectrometry of oligonucleotide complexes with drugs, metals, and proteins

Beck

Colgrave

Ralph

et al. 2001

Mass Spectrometry Reviews

227

204

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I. Introduction 61 II. Binding of Small Molecules to DNA 62 A. Covalent Binding 62 B. Reversible (Noncovalent) DNA-Binding Agents 65 III. DNA-Metal Ion Complexes 67 A. Platinum Complexes 70 B. Other Metal Ions 73 IV. DNA-Protein Complexes 74 A. Introduction 74 B. ESI-MS of DNA-Protein Complexes 76 C. ESI-MS Analysis of Proteolytic Products of DNA-Protein Complexes 79 D. ESI-MS of Ternary DNA-Protein-Ligand Complexes 80 V. Conclusions 80 Abbreviations 81 References 81 --Interactions 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. (c) 2001 John Wiley & Sons, Inc.

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confidence: 99%

Electrospray ionization mass spectrometry of oligonucleotide complexes with drugs, metals, and proteins

Beck

Colgrave

Ralph

et al. 2001

Mass Spectrometry Reviews

227

204

View full text Add to dashboard Cite

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“…Second, competition experiments can be used to evaluate the stability of noncovalent complexes. In Jørgensen's method [23,24], the relative intensities of the free host and the different complexes were used, whereas Kempen et al employed the known concentration of a reference complex to determine the concentration of an unknown complex [25]. Third, a titration of a host with a guest (or vice versa) can be used.…”

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confidence: 99%

Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors

Daniel

McCombie

Wendt

et al. 2003

J. Am. Soc. Mass Spectrom.

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Noncovalent complexes between chicken muscle adenylate kinase and two inhibitors, P 1 ,P 4 -di(adenosine-5')tetraphosphate (Ap4A) and P 1 ,P 5 -di(adenosine-5') pentaphosphate (Ap5A), were investigated with electrospray ionization mass spectrometry under non-denaturing conditions. The nonconvalent nature and the specificity of the complexes are demonstrated with a number of control experiments. Titration experiments allowed the association constants for inhibitor binding to be determined. Problems with concentration dependent ion yields are circumvented by a data evaluation method that is insensitive to the overall ionization efficiency. The K a values found were 9.0 ϫ 10 4 M Ϫ1 (Ap4A) and 4.0 ϫ S oft ionization mass spectrometry (MS), in particular matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI), is well known for its ability to bring high molecular weight biomolecules into the gase phase and to even preserve noncovalent complexes [1][2][3][4][5][6][7][8][9][10]. Besides its established applications, a recurring question concerns the applicability of mass spectrometry to measuring noncovalent interaction strengths [11]. There are different approaches to measure the interaction strengths in the gas phase as well as in the liquid phase. In the former case, the mass spectra should ideally directly represent the solution phase chemistry. Gas-phase methods include cone voltage driven dissociation (called the "VC 50 " method) [12,13], collision-induced dissociation [14,15], guided ion beam tandem mass spectrometry [16,17], blackbody infrared radiative dissociation [18,19] and heated capillary dissocation [20,21].Some mass spectrometric studies have been reported in the literature for the determination of noncovalent interaction strengths. There are three basic methods to determine association constants that are reflective of those in solution: first, it is possible to record "melting curves" by raising the temperature of the analyte solution and to use MS to determine the percentage of intact complexes. Cheng et al. analyzed complementary DNA strands [22] and Fändrich et al. studied the chaperone GimC/prefolding homologue complex [13] with this method. Second, competition experiments can be used to evaluate the stability of noncovalent complexes. In Jørgensen's method [23,24], the relative intensities of the free host and the different complexes were used, whereas Kempen et al. employed the known concentration of a reference complex to determine the concentration of an unknown complex [25]. Third, a titration of a host with a guest (or vice versa) can be used. In this case, the mass spectrometric signals should accurately represent the concentrations of the species in solution. The titration method is documented in a number of publications, all of them convincingly showing the successful use of mass spectrometry for the quantitative determination of noncovalent binding constants of proteins and small molecules [26 -33]. This aspect was the main focus in most previous research; th...

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“…For instance, it has been reported that CDP-I has no antibacterial activity (30). Previously we have shown that electrospray ionization can be used quantitatively to determine solution-phase association constants between vancomycin group antibiotics and bacterial cell wall receptor analogues (3,25,26,33,34). The bioaffinity ESI-MS method relies on the assumption that the antibiotics and their noncovalent complexes with the receptor-mimicking peptides have relatively the same ionization efficiencies.…”

Section: Determination Of Association Constants Using Nanoelectrospramentioning

confidence: 99%

Formation and Efficacy of Vancomycin Group Glycopeptide Antibiotic Stereoisomers Studied by Capillary Electrophoresis and Bioaffinity Mass Spectrometry

Bonnici¹,

Damen²,

Waterval

et al. 2001

Analytical Biochemistry

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Subtle differences in molecular recognition between modified glycopeptide antibiotics and bacterial receptor peptides identified by electrospray ionization mass spectrometry

Cited by 39 publications

References 26 publications

Electrospray ionization mass spectrometry of oligonucleotide complexes with drugs, metals, and proteins

Electrospray ionization mass spectrometry of oligonucleotide complexes with drugs, metals, and proteins

Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors

Formation and Efficacy of Vancomycin Group Glycopeptide Antibiotic Stereoisomers Studied by Capillary Electrophoresis and Bioaffinity Mass Spectrometry

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