Characterization of microcystins using in‐source collision‐induced dissociation

Kubwabo, Cariton; Vais, Natalia; Benoit, Frank M.

doi:10.1002/rcm.1828

Cited by 37 publications

(30 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…c-Type fragmentation of the precursor b-ions is mechanistically possible and has been described for microcystins [46], [47]. The same holds true for z-like fragments [47], which in the case of cyclic peptides are equal to y-like-NH 3 or b-NH 3 ions with respect to their sum formula.…”

Section: Methodsmentioning

confidence: 80%

“…The fragmentation behavior of microcystins, cyclic heptapeptides found in several cyanobacterial genera, has been well studied [46], [47], [60], [80], [81]. Thus microcystin LF has been used to examine the accuracy and comprehensiveness of our fragmentation algorithms.…”

Section: Results and Discussion: Evaluation Of The Softwarementioning

confidence: 99%

“…Loss of H 2 O or NH 3 is a common phenomenon found for cyclic peptides, even if no hydroxyl groups are present in the molecule [40], [44], [46], [48], [60]–[64]. Loss of H 2 O and NH 3 at the same time is possible, and also side chain neutral losses in conjunction with H 2 O or NH 3 losses have been observed [27], [45], [47].…”

Section: Methodsmentioning

confidence: 99%

“…They are less frequently observed for low-energy CID [23], [69], [70], but several side chain neutral losses have also been described for this dissociation technique, e.g. neutral losses from arginine [47], [71]–[73], the non-proteinogenic amino acid Adda ((2S,3S,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyl-deca-4,6-dienoic acid) [46], [47] or other modified amino acids [74]. Due to the possible occurrence of these losses, mMass now gives the user the possibility to freely define side chain neutral losses.…”

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

mMass as a Software Tool for the Annotation of Cyclic Peptide Tandem Mass Spectra

2012

View full text Add to dashboard Cite

Natural or synthetic cyclic peptides often possess pronounced bioactivity. Their mass spectrometric characterization is difficult due to the predominant occurrence of non-proteinogenic monomers and the complex fragmentation patterns observed. Even though several software tools for cyclic peptide tandem mass spectra annotation have been published, these tools are still unable to annotate a majority of the signals observed in experimentally obtained mass spectra. They are thus not suitable for extensive mass spectrometric characterization of these compounds. This lack of advanced and user-friendly software tools has motivated us to extend the fragmentation module of a freely available open-source software, mMass (http://www.mmass.org), to allow for cyclic peptide tandem mass spectra annotation and interpretation. The resulting software has been tested on several cyanobacterial and other naturally occurring peptides. It has been found to be superior to other currently available tools concerning both usability and annotation extensiveness. Thus it is highly useful for accelerating the structure confirmation and elucidation of cyclic as well as linear peptides and depsipeptides.

show abstract

Section: Methodsmentioning

confidence: 80%

Section: Results and Discussion: Evaluation Of The Softwarementioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

mMass as a Software Tool for the Annotation of Cyclic Peptide Tandem Mass Spectra

2012

View full text Add to dashboard Cite

show abstract

“…In addition to the advantages of the technique as a whole,18 ESI offers the possibility of controlling the degree of ion excitation by changing the potential between the capillary or nozzle and the skimmer in the ESI source 9, 10, 17–42. In different publications this potential is referred to as the declustering potential,30 orifice potential,10 capillary‐skimmer,31 needle‐skimmer,9 nozzle‐skimmer19, 34 potential, or sampling cone voltage (CV) 10, 37–42.…”

mentioning

confidence: 99%

The effect of cone voltage on electrospray mass spectra of the bisquaternary ammonium salt decamethoxinum

Pashynska

Kosevich

Heuvel

et al. 2006

Rapid Comm Mass Spectrometry

View full text Add to dashboard Cite

The effect of cone voltage (CV) variation on the mass spectral pattern of the bisquaternary ammonium salt decamethoxinum in the electrospray ionization (ESI) mode was studied. The advantage of decamethoxinum as a test compound in ESI mass spectrometry lies in the production of two types of precursor ions, i.e. the doubly charged organic dication Cat 2R and its singly charged cluster with a Cl S counterion, Cat Á Cl R . This makes it possible to monitor the fragmentation patterns of these ions under identical experimental conditions. Pronounced qualitative and quantitative changes in the ESI mass spectra were observed upon a gradual increase of the CV. The model compound decamethoxinum allowed us to reveal the extreme situation, in which the mass spectra at a CV below and over approximately 100 V look quite different, in that they contain different product ions of Cat 2R and Cat Á Cl R . While this effect may be much less pronounced for other classes of organic compounds, it should be properly taken into account for the adequate description of fragmentation pathways of bisquaternary ammonium compounds with ESI. Comparison of ESI, FAB-SIMS and MALDI mass spectra of decamethoxinum shows that taking into account CV effects also permits us to gain information on energy deposition into ions generated with the different ionization techniques. 10,[37][38][39][40][41][42] It is believed that the CV effect is due to an in-source collision-induced dissociation (CID) (up-front CID) process. The initially sprayed charged species can undergo collisions with the residual or bath gas on their path between the nozzle and the skimmer, and the change of the ion velocity caused by CV variation affects their kinetic energy and, consequently, their collision energy. 18The possibility of controlling the charge state of the ions, the desolvation process and the degree of fragmentation of the ions by CV variation offers the prospect of many useful applications of this technique, mainly in studies of supramolecular noncovalent complexes. [25][26][27][28][29][30][31][32][33][34][35][36] For example, a method was suggested for evaluating the stability of chemotherapeutic non-intercalating drugs binding to DNA on the basis of monitoring DNA-drug complex decomposition upon CV increase, which correlates with the thermal decomposition of the complex. 25,26 CV adjustment is also of critical importance in probing the structures of surfactant micelles generated under ESI conditions. 30,31 In-source CID is used along with collision-cell tandem mass spectrometric (MS/MS) CID in studies of protein structures. [19][20][21][32][33][34][35][36] Comparison of in-cell CID and in-source CID 32 permits us to obtain more comprehensive information on the molecular structures of analytes. A method, denoted as energydependent ESI mass spectrometry (EDESI-MS), employing CV variation, has been reported for fragmentation studies of metalloorganic compounds.

show abstract