Gas-Phase Helical Peptides Mimic Solution-Phase Behavior

2014 ◽  
Vol 136 (40) ◽  
pp. 14173-14183 ◽  
Author(s):  
Lindsay J. Morrison ◽  
Vicki H. Wysocki
2008 ◽  
Vol 22 (24) ◽  
pp. 4089-4097 ◽  
Author(s):  
Linda M. M. Weigang ◽  
Dieter Langosch ◽  
Thomas Letzel

2018 ◽  
Vol 14 (4) ◽  
pp. 305-315 ◽  
Author(s):  
Sujata D. Sakhare ◽  
V. Sai Krishna Anand ◽  
Aishwarya Karan ◽  
K. Navya Sree ◽  
S. G. Vasantharaju ◽  
...  

2007 ◽  
Vol 10 (4) ◽  
pp. 553 ◽  
Author(s):  
Kalyuzhnyi ◽  
Protsykevitch ◽  
Cummings

2015 ◽  
Vol 119 (50) ◽  
pp. 11989-11996 ◽  
Author(s):  
Michael D. Horbury ◽  
Lewis A. Baker ◽  
Wen-Dong Quan ◽  
Jamie D. Young ◽  
Michael Staniforth ◽  
...  
Keyword(s):  

1997 ◽  
Vol 73 (6) ◽  
pp. 3078-3088 ◽  
Author(s):  
S. Morein ◽  
E. Strandberg ◽  
J.A. Killian ◽  
S. Persson ◽  
G. Arvidson ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5280
Author(s):  
Chris Furlan ◽  
Jacob A. Berenbeim ◽  
Caroline E. H. Dessent

Verteporfin, a free base benzoporphyrin derivative monoacid ring A, is a photosensitizing drug for photodynamic therapy (PDT) used in the treatment of the wet form of macular degeneration and activated by red light of 689 nm. Here, we present the first direct study of its photofragmentation channels in the gas phase, conducted using a laser interfaced mass spectrometer across a broad photoexcitation range from 250 to 790 nm. The photofragmentation channels are compared with the collision-induced dissociation (CID) products revealing similar dissociation pathways characterized by the loss of the carboxyl and ester groups. Complementary solution-phase photolysis experiments indicate that photobleaching occurs in verteporfin in acetonitrile; a notable conclusion, as photoinduced activity in Verteporfin was not thought to occur in homogenous solvent conditions. These results provide unique new information on the thermal break-down products and photoproducts of this light-triggered drug.


2005 ◽  
Vol 83 (11) ◽  
pp. 1953-1960 ◽  
Author(s):  
Belal M Hossain ◽  
Douglas A Simmons ◽  
Lars Konermann

Electrospray ionization (ESI) mass spectrometry (MS) has become a popular tool for monitoring ligand–protein and protein–protein interactions. Due to the "gentle" nature of the ionization process, it is often possible to transfer weakly bound complexes into the gas phase, thus making them amenable to MS detection. One problem with this technique is the potential occurrence of fragmentation events during ESI. Also, some analytes tend to cluster together during ionization, thus forming nonspecific gas-phase assemblies that do not represent solution-phase complexes. In this work, we implemented a hydrogen–deuterium exchange (HDX) approach that can reveal whether or not the free and (or) bound constituents of a complex observed in ESI-MS reflect the binding situation in solution. Proteins are subjected to ESI immediately following an isotopic labeling pulse; only ligand-free and ligand-bound protein ions that were formed directly from the corresponding solution-phase species showed different HDX levels. Using myoglobin as a model system, it is demonstrated that this approach can readily distinguish scenarios where the heme–protein interactions were disrupted in solution from those where dissociation of the complex occurred in the gas phase. Experiments on cytochrome c strongly suggest that dimeric protein ions observed in ESI-MS reflect aggregates that were formed in solution.Key words: electrospray mass spectrometry, ligand–protein interaction, noncovalent complex, hydrogen–deuterium exchange, protein folding.


Sign in / Sign up

Export Citation Format

Share Document