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Comparison of CID spectra of singly charged polypeptide antibiotic precursor ions obtained by positive-ion vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT mass spectrometry.
J Mass Spectrom. 2006 Apr; 41(4):421-47.JM

Abstract

Various classes of polypeptide antibiotics, including blocked linear peptides (gramicidin D), side-chain-cyclized peptides (bacitracin, viomycin, capreomycin), side-chain-cyclized depsipeptides (virginiamycin S), real cyclic peptides (tyrocidin, gramcidin S) and side-chain-cyclized lipopeptides (polymyxin B and E, amfomycin), were investigated by low-energy collision induced dissociation (LE-CID) as well as high-energy CID (HE-CID). Ion trap (IT) based instruments with different desorption/ionization techniques such as electrospray ionization (ESI), atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) and vacuum MALDI (vMALDI) as well as a vMALDI-time-of-flight (TOF)/curved field-reflectron instrument fitted with a gas collision cell were used. For optimum comparability of data from different IT instruments, the CID conditions were standardized and only singly charged precursor ions were considered. Additionally, HE-CID data obtained from the TOF-based instrument were acquired and compared with LE-CID data from ITs. Major differences between trap-based and TOF-based CID data are that the latter data set lacks abundant additional loss of small neutrals (e.g. ammonia, water) but contains product ions down to the immonium-ion-type region, thereby allowing the detection of even single amino-acid (even unusual amino acids) substitutions. For several polypeptide antibiotics, mass spectrometric as well as tandem mass spectrometric data are shown and discussed for the first time, and some yet undescribed minor components are also reported. De novo sequencing of unusually linked minor components of (e.g. cyclic) polypeptides is practically impossible without knowledge of the exact structure and fragmentation behavior of the major components. Finally, the described standardized CID condition constitutes a basic prerequisite for creating a searchable, annotated MS(n)-database of bioactive compounds. The applied desorption/ionization techniques showed no significant influence on the type of product ions (neglecting relative abundances of product ions formed) observed, and therefore the type of analyzer connected with the CID process mainly determines the type of fragment ions.

Authors+Show Affiliations

Institute of Chemical Technologies and Analytics, Vienna University of Technology, Vienna, Austria.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16604520

Citation

Pittenauer, Ernst, et al. "Comparison of CID Spectra of Singly Charged Polypeptide Antibiotic Precursor Ions Obtained By Positive-ion Vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT Mass Spectrometry." Journal of Mass Spectrometry : JMS, vol. 41, no. 4, 2006, pp. 421-47.
Pittenauer E, Zehl M, Belgacem O, et al. Comparison of CID spectra of singly charged polypeptide antibiotic precursor ions obtained by positive-ion vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT mass spectrometry. J Mass Spectrom. 2006;41(4):421-47.
Pittenauer, E., Zehl, M., Belgacem, O., Raptakis, E., Mistrik, R., & Allmaier, G. (2006). Comparison of CID spectra of singly charged polypeptide antibiotic precursor ions obtained by positive-ion vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT mass spectrometry. Journal of Mass Spectrometry : JMS, 41(4), 421-47.
Pittenauer E, et al. Comparison of CID Spectra of Singly Charged Polypeptide Antibiotic Precursor Ions Obtained By Positive-ion Vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT Mass Spectrometry. J Mass Spectrom. 2006;41(4):421-47. PubMed PMID: 16604520.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comparison of CID spectra of singly charged polypeptide antibiotic precursor ions obtained by positive-ion vacuum MALDI IT/RTOF and TOF/RTOF, AP-MALDI-IT and ESI-IT mass spectrometry. AU - Pittenauer,Ernst, AU - Zehl,Martin, AU - Belgacem,Omar, AU - Raptakis,Emmanuel, AU - Mistrik,Robert, AU - Allmaier,Günter, PY - 2006/4/11/pubmed PY - 2007/7/12/medline PY - 2006/4/11/entrez SP - 421 EP - 47 JF - Journal of mass spectrometry : JMS JO - J Mass Spectrom VL - 41 IS - 4 N2 - Various classes of polypeptide antibiotics, including blocked linear peptides (gramicidin D), side-chain-cyclized peptides (bacitracin, viomycin, capreomycin), side-chain-cyclized depsipeptides (virginiamycin S), real cyclic peptides (tyrocidin, gramcidin S) and side-chain-cyclized lipopeptides (polymyxin B and E, amfomycin), were investigated by low-energy collision induced dissociation (LE-CID) as well as high-energy CID (HE-CID). Ion trap (IT) based instruments with different desorption/ionization techniques such as electrospray ionization (ESI), atmospheric pressure matrix-assisted laser desorption/ionization (AP-MALDI) and vacuum MALDI (vMALDI) as well as a vMALDI-time-of-flight (TOF)/curved field-reflectron instrument fitted with a gas collision cell were used. For optimum comparability of data from different IT instruments, the CID conditions were standardized and only singly charged precursor ions were considered. Additionally, HE-CID data obtained from the TOF-based instrument were acquired and compared with LE-CID data from ITs. Major differences between trap-based and TOF-based CID data are that the latter data set lacks abundant additional loss of small neutrals (e.g. ammonia, water) but contains product ions down to the immonium-ion-type region, thereby allowing the detection of even single amino-acid (even unusual amino acids) substitutions. For several polypeptide antibiotics, mass spectrometric as well as tandem mass spectrometric data are shown and discussed for the first time, and some yet undescribed minor components are also reported. De novo sequencing of unusually linked minor components of (e.g. cyclic) polypeptides is practically impossible without knowledge of the exact structure and fragmentation behavior of the major components. Finally, the described standardized CID condition constitutes a basic prerequisite for creating a searchable, annotated MS(n)-database of bioactive compounds. The applied desorption/ionization techniques showed no significant influence on the type of product ions (neglecting relative abundances of product ions formed) observed, and therefore the type of analyzer connected with the CID process mainly determines the type of fragment ions. SN - 1076-5174 UR - https://www.unboundmedicine.com/medline/citation/16604520/Comparison_of_CID_spectra_of_singly_charged_polypeptide_antibiotic_precursor_ions_obtained_by_positive_ion_vacuum_MALDI_IT/RTOF_and_TOF/RTOF_AP_MALDI_IT_and_ESI_IT_mass_spectrometry_ L2 - https://doi.org/10.1002/jms.1032 DB - PRIME DP - Unbound Medicine ER -