Exploring the coordination chemistry of isomerizable terpyridine derivatives for successful analyses of cis and trans isomers by travelling wave ion mobility mass spectrometry

The Analyst ◽  
2012 ◽  
Vol 137 (17) ◽  
pp. 4045 ◽  
Author(s):  
Jonnatan J. Santos ◽  
Sergio H. Toma ◽  
Priscila M. Lalli ◽  
Maria F. Riccio ◽  
Marcos N. Eberlin ◽  
...  
Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4539
Author(s):  
Nguyen Minh Thuy ◽  
Vo Minh ◽  
Tran Ben ◽  
My Tuyen Thi Nguyen ◽  
Ho Ha ◽  
...  

Butterfly pea flower have great sensory attraction, but they have not yet been used widely in Vietnam. Extracts of butterfly pea flowers can be used conveniently as a natural blue colorant for food products. In this study, the identification of anthocyanin compounds in butterfly pea flowers was performed by UPLC coupled with a UV and Mass spectrometer instrument. Positive and negative ion electrospray MS/MS chromatograms and spectra of the anthocyanin compounds were determined. By analyzing the chromatograms and spectra for each ion, five anthocyanins were identified in the butterfly pea flower extract; these were delphinidin-3-(6”‐p-coumaroyl)-rutinoside, cyanidin 3-(6”-p-coumaroyl)-rutinoside, delphinidin-3-(p-coumaroyl) glucose in both cis- and trans- isomers, cyanidin-3-(p-coumaroyl-glucoside) and delphinidin-3-pyranoside. Additionally, based on their intensity, it was determined that cyanidin-3-(p-coumaroyl-glucoside) was the most abundant anthocyanin, followed by cyanidin 3-(6”-p-coumaroyl)-rutinoside, delphinidin-3-(p-coumaroyl-glucoside), delphinidin-3-(6”-p-coumaroyl)-rutinoside and delphinidin-3-pyranoside. In this study, cyanidin derivatives were discovered in butterfly pea flower extract, where these compounds had not been detected in previous studies.


2013 ◽  
Vol 345-347 ◽  
pp. 54-62 ◽  
Author(s):  
Ganesh N. Sivalingam ◽  
Jun Yan ◽  
Harpal Sahota ◽  
Konstantinos Thalassinos

2012 ◽  
Vol 65 (5) ◽  
pp. 504 ◽  
Author(s):  
Antonio N. Calabrese ◽  
Lauren A. Speechley ◽  
Tara L. Pukala

This study demonstrates the ability of travelling wave ion mobility-mass spectrometry to measure collision cross-sections of ions in the negative mode, using a calibration based approach. Here, negative mode ion mobility-mass spectrometry was utilised to understand structural transitions of calmodulin upon Ca2+ binding and complexation with model peptides melittin and the plasma membrane Ca2+ pump C20W peptide. Coexisting calmodulin conformers were distinguished on the basis of their mass and cross-section, and identified as relatively folded and unfolded populations, with good agreement in collision cross-section to known calmodulin geometries. Titration of calcium tartrate to physiologically relevant Ca2+ levels provided evidence for intermediately metalated species during the transition from apo- to holo-calmodulin, with collision cross-section measurements indicating that higher Ca2+ occupancy is correlated with more compact structures. The binding of two representative peptides which exemplify canonical compact (melittin) and extended (C20W) peptide-calmodulin binding models has also been interrogated by ion mobility mass spectrometry. Peptide binding to calmodulin involves intermediates with metalation states from 1–4 Ca2+, which demonstrate relatively collapsed structures, suggesting neither the existence of holo-calmodulin or a pre-folded calmodulin conformation is a prerequisite for binding target peptides or proteins. The biological importance of the different metal unsaturated calmodulin complexes, if any, is yet to be understood.


2016 ◽  
Vol 51 (11) ◽  
pp. 1064-1079 ◽  
Author(s):  
David J. Harvey ◽  
Charlotte A. Scarff ◽  
Matthew Edgeworth ◽  
Kevin Pagel ◽  
Konstantinos Thalassinos ◽  
...  

2012 ◽  
Vol 26 (3) ◽  
pp. 263-268 ◽  
Author(s):  
Priscila M. Lalli ◽  
Bernardo A. Iglesias ◽  
Daiana K. Deda ◽  
Henrique E. Toma ◽  
Gilberto F. Sa ◽  
...  

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