Development of an ESI-MS screening method for evaluating binding affinity between integrin fragments and RGD-based peptides

Raji, Misjudeen; Fryčák, Petr; Beall, M. L.; Sakrout, Mohamed; Ahn, Jung Mo; Yu, Bo; Armstrong, Daniel W.; Schug, Kevin A.

doi:10.1016/j.ijms.2006.11.015

Cited by 19 publications

(16 citation statements)

References 24 publications

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“…Thus, ESI-MS should be used to determine relative binding affinities rather than absolute values. 341,343,344 K d values obtained by MS should be used with caution in the absence of validation from other solution-phase techniques. 343 …”

Section: Characterization Of Protein Binding To Arsenic Speciesmentioning

confidence: 99%

Arsenic Binding to Proteins

Shen

Li²,

Cullen³

et al. 2013

Chem. Rev.

683

576

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Section: Characterization Of Protein Binding To Arsenic Speciesmentioning

confidence: 99%

Arsenic Binding to Proteins

Shen

Li²,

Cullen³

et al. 2013

Chem. Rev.

683

576

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“…Response factors may also change with pH, further complicating quantitation [89]. This represents one of the biggest disadvantages of the ESI-MS method for binding-constant determination [90]. The influence of response factors has been discussed in detail [91].…”

Section: Electrospray Ionization Mass Spectrometrymentioning

confidence: 99%

Determination of binding constants by affinity capillary electrophoresis, electrospray ionization mass spectrometry and phase-distribution methods

Chen

Weber

2008

TrAC Trends in Analytical Chemistry

130

108

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Many methods for determining intermolecular interactions have been described in the literature in the past several decades. Chief among them are methods based on spectroscopic changes, particularly those based on absorption or nuclear magnetic resonance (NMR) [especially proton NMR ( 1 H NMR)]. Recently, there have been put forward several new methods that are particularly adaptable, use very small quantities of material, and do not place severe requirements on the spectroscopic properties of the binding partners. This review covers new developments in affinity capillary electrophoresis, electrospray ionization mass spectrometry (ESI-MS) and phasetransfer methods.

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“…MS offers several advantages over other analytical methods including speed, sensitivity, and exact stoichiometric measurement. Raji et al40 have utilized electrospray MS (ESI‐MS) to evaluate binding affinities between integrin fragments and RGD‐based peptide ligands. Frontal analysis CE (FACE) was used as a complementary solution phase technique to measure binding constants and was compared to the ESI‐MS technique.…”

Section: Discussionmentioning

confidence: 99%