Thermochemistry of Non-Covalent Ion–Molecule Interactions

Armentrout, P. B.; Rodgers, M. T.

doi:10.5702/massspectrometry.s0005

Cited by 5 publications

(3 citation statements)

References 79 publications

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“…H‐G complexes have been subjected to various mass spectrometry‐based studies with a variety of purposes such as measurement of the energetics of H‐G binding using blackbody infrared radiative dissociation (BIRD) or threshold collision induced dissociation (TCID), obtaining a relative ranking of the stabilities of H‐G complexes by comparing fragmentation efficiency (or survival yield [SY]) curves, studying the role of proton affinities of guest molecules on the characteristics of fragmentation spectra of H‐G complexes, exploring the structure of H‐G complexes and the interactions between the two partners using the Förster resonance energy transfer (FRET) technique, quantifying binding affinities by mass spectrometric titration, and exploring the influence of solvent on H‐G affinities . These kinds of gas‐phase studies, however, have been never employed for the study of hemicryptophane H‐G complexes.…”

Section: Introductionmentioning

confidence: 99%

Investigation of activation energies for dissociation of host‐guest complexes in the gas phase using low‐energy collision induced dissociation

et al. 2019

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A low‐energy collision induced dissociation (CID) (low‐energy CID) approach that can determine both activation energy and activation entropy has been used to evaluate gas‐phase binding energies of host‐guest (H‐G) complexes of a heteroditopic hemicryptophane cage host (Zn (II)@1) with a series of biologically relevant guests. In order to use this approach, preliminary calibration of the effective temperature of ions undergoing resonance excitation is required. This was accomplished by employing blackbody infrared radiative dissociation (BIRD) which allows direct measurement of activation parameters. Activation energies and pre‐exponential factors were evaluated for more than 10 H‐G complexes via the use of low‐energy CID. The relatively long residence time of the ions inside the linear ion trap (maximum of 60 s) allowed the study of dissociations with rates below 1 s−1. This possibility, along with the large size of the investigated ions, ensures the fulfilment of rapid energy exchange (REX) conditions and, as a consequence, accurate application of the Arrhenius equation. Compared with the BIRD technique, low‐energy CID allows access to higher effective temperatures, thereby permitting one to probe more endothermic decomposition pathways. Based on the measured activation parameters, guests bearing a phosphate (―OPO32−) functional group were found to bind more strongly with the encapsulating cage than those having a sulfonate (―SO3−) group; however, the latter ones make stronger bonds than those with a carboxylate (―CO2−) group. In addition, it was observed that the presence of trimethylammonium (―N(CH3)3+) or phenyl groups in the guest's structure improves the strength of H‐G interactions. The use of this technique is very straightforward, and it does not require any instrumental modifications. Thus, it can be applied to other H‐G chemistry studies where comparison of bond dissociation energies is of paramount importance.

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Section: Introductionmentioning

confidence: 99%

Investigation of activation energies for dissociation of host‐guest complexes in the gas phase using low‐energy collision induced dissociation

et al. 2019

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“…When comparing the BDEs of the five alkali cations to any particular ligand, one finds that the values increase as the size of the metal cation decreases. [123][124][125] This is a simple electrostatic effect in that the smaller cation has a shorter bond distance leading to a stronger bond. Glycine, or for that matter any other amino acid or small peptide, is no exception.…”

Section: Periodic Trends In Binding Energiesmentioning

confidence: 99%

Perspective: intrinsic interactions of metal ions with biological molecules as studied by threshold collision-induced dissociation and infrared multiple photon dissociation

Armentrout

2024

Phys. Chem. Chem. Phys.

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“…By contrast, up to now there exists no mass spectrometric method which has gained equal acceptance for investigating gas phase binding strengths of distinct protein-ligand complexes. Previous reports have shown that high pressure mass spectrometry and/or black body irradiation can be applied for analyzing small molecule-ion equilibria and to determine kinetic and thermodynamic properties, such as ion-ligand complex constants in the right order of magnitude [ 2 , 3 , 4 ] also for small peptides, the protonated glycine dimer being the smallest possible peptide dimer representative [ 5 ]. Gas phase dissociation reactions of Leu-enkephaline dimers [ 6 ] and of small proteins, such as ubiquitin [ 7 ] had been studied as well.…”

Section: Introductionmentioning

confidence: 99%

Mass Spectrometric Analysis of Antibody—Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization

et al. 2020

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Electrospray mass spectrometry is applied to determine apparent binding energies and quasi equilibrium dissociation constants of immune complex dissociation reactions in the gas phase. Myoglobin, a natural protein-ligand complex, has been used to develop the procedure which starts from determining mean charge states and normalized and averaged ion intensities. The apparent dissociation constant KD m0g#= 3.60 × 10−12 for the gas phase heme dissociation process was calculated from the mass spectrometry data and by subsequent extrapolation to room temperature to mimic collision conditions for neutral and resting myoglobin. Similarly, for RNAse S dissociation at room temperature a KD m0g#= 4.03 × 10−12 was determined. The protocol was tested with two immune complexes consisting of epitope peptides and monoclonal antibodies. For the epitope peptide dissociation reaction of the FLAG peptide from the antiFLAG antibody complex an apparent gas phase dissociation constant KD m0g#= 4.04 × 10−12 was calculated. Likewise, an apparent KD m0g#= 4.58 × 10−12 was calculated for the troponin I epitope peptide—antiTroponin I antibody immune complex dissociation. Electrospray mass spectrometry is a rapid method, which requires small sample amounts for either identification of protein-bound ligands or for determination of the apparent gas phase protein-ligand complex binding strengths.

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Thermochemistry of Non-Covalent Ion–Molecule Interactions

Cited by 5 publications

References 79 publications

Investigation of activation energies for dissociation of host‐guest complexes in the gas phase using low‐energy collision induced dissociation

Investigation of activation energies for dissociation of host‐guest complexes in the gas phase using low‐energy collision induced dissociation

Perspective: intrinsic interactions of metal ions with biological molecules as studied by threshold collision-induced dissociation and infrared multiple photon dissociation

Mass Spectrometric Analysis of Antibody—Epitope Peptide Complex Dissociation: Theoretical Concept and Practical Procedure of Binding Strength Characterization

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