Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

9.0K Views

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11:04 min

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September 7th, 2019

DOI :

10.3791/60102-v

September 7th, 2019

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8,972 Views

Enas N. Yousef¹, Ramakrishna Sesham¹, Jacob W. McCabe¹, Rajpal Vangala¹, Laurence A. Angel¹

¹Department of Chemistry, Texas A&M University-Commerce

Chapitres

0:04

Title

0:58

Electrospray-ion Mobility-Mass Spectrometry Analysis

3:02

Analysis of ESI-IM-MS pH Titration Data

6:11

Collision Cross-Sections and Computational Methods

8:30

Results: Reaction Mechanisms and Coordination Sites of the Alternative Methanobactin Complexes

10:00

Conclusion

Transcription

Ion mobility-mass spectrometry, or IM-MS, identify the various products ions from the pH-dependent redox and methyl binding reaction of peptides. With the molecular modeling of their tertiary structure, metal correlation can be determined. IM-MS c

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Résumé

Ion mobility-mass spectrometry and molecular modeling techniques can characterize the selective metal chelating performance of designed metal-binding peptides and the copper-binding peptide methanobactin. Developing new classes of metal chelating peptides will help lead to therapeutics for diseases associated with metal ion misbalance.

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Ion Mobility mass Spectrometry

IM MS

Metal Ion Recognition

Redox Activity

Metal Binding Oligopeptides

Alternative Methanobactin