Cation-radicals and dications corresponding to hydrogen atom adducts to N-terminus-protonated N(alpha)-glycylphenylalanine amide (Gly-Phe-NH(2)) are studied by combined density functional theory and Møller-Plesset perturbational computations (B3-MP2) as models for electron-capture dissociation of peptide bonds and elimination of side-chain groups in gas-phase peptide ions. Several structures are identified as local energy minima including isomeric aminoketyl cation-radicals, and hydrogen-bonded ion-radicals, and ylid-cation-radical complexes. The hydrogen-bonded complexes are substantially more stable than the classical aminoketyl structures. Dissociations of the peptide N-C(alpha) bonds in aminoketyl cation-radicals are 18-47 kJ mol(-1) exothermic and require low activation energies to produce ion-radical complexes as stable intermediates. Loss of the side-chain benzyl group is calculated to be 44 kJ mol(-1) endothermic and requires 68 kJ mol(-1) activation energy. Rice-Ramsperger-Kassel-Marcus (RRKM) and transition-state theory (TST) calculations of unimolecular rate constants predict fast preferential N-C(alpha) bond cleavage resulting in isomerization to ion-molecule complexes, while dissociation of the C(alpha)bond;CH(2)C(6)H(5) bond is much slower. Because of the very low activation energies, the peptide bond dissociations are predicted to be fast in peptide cation-radicals that have thermal (298 K) energies and thus behave ergodically.
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http://dx.doi.org/10.1002/jms.527 | DOI Listing |
Molecules
March 2024
Functional Dairy Products Engineering Laboratory of Gansu Province, College of Food Science and Engineering, Gansu Agricultural University, Anning District, Lanzhou 730070, China.
Yak whey protein concentrates (YWPCs) have good functional properties, but there is still a gap in the study of their peptides. In this study, peptides were obtained by enzymatic hydrolysis, and the bioactivity of each ultrafiltration fraction was evaluated using an optimal process. YWPCs were isolated and purified from yak milk as the raw material.
View Article and Find Full Text PDFJ Agric Food Chem
December 2018
Department of Analytical Chemistry, Faculty of Chemical Engineering and Technology, Institute C-1 , Cracow University of Technology, ul. Warszawska 24 , Cracow 31-155 , Poland.
Formation of glutathionic conjugates with quinonoid forms generated through oxidation of betanidin and gomphrenin obtained from fruits of Basella alba L. was studied by high-performance liquid chromatography coupled with triple quadrupole tandem mass spectrometry (HPLC-DAD-ESI-MS/MS) and ion-trap time-of-flight high-resolution mass spectrometry (LCMS-IT-TOF). The conjugates were studied for the aim of trapping the formed quinonoids by glutathione which would indicate a presence of specific quinonoid structures in reaction products of the pigments with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) cation radicals.
View Article and Find Full Text PDFJ Am Soc Mass Spectrom
September 2018
Department of Chemistry, University of Washington, Box 351700, Seattle, WA, 98195-1700, USA.
Peptide cation radicals of the z-type were produced by electron transfer dissociation (ETD) of peptide dications and studied by UV-Vis photodissociation (UVPD) action spectroscopy. Cation radicals containing the Asp (D), Asn (N), Glu (E), and Gln (Q) residues were found to spontaneously isomerize by hydrogen atom migrations upon ETD. Canonical N-terminal [z + H] fragment ion-radicals of the R-CH-CONH- type, initially formed by N-C bond cleavage, were found to be minor components of the stable ion fraction.
View Article and Find Full Text PDFJ Mass Spectrom
February 2018
Department of Chemistry, University of Washington, Bagley Hall, Box 351700, Seattle, WA, 98195-1700, USA.
We report non-chiral amino acid residues cis- and trans-1,4-diaminocyclohexane-1-carboxylic acid (cyclo-ornithine, cO) that exhibit unprecedented stereospecific control of backbone dissociations of singly charged peptide cations and hydrogen-rich cation radicals produced by electron-transfer dissociation. Upon collision-induced dissociation (CID) in the slow heating regime, peptide cations containing trans-cO residues undergo facile backbone cleavages of amide bonds C-terminal to trans-cO. By contrast, peptides with cis-cO residues undergo dissociations at several amide bonds along the peptide ion backbone.
View Article and Find Full Text PDFJ Phys Chem B
July 2017
Department of Chemistry, University of Washington, Bagley Hall, Box 351700, Seattle, Washington 98195-1700, United States.
Peptide cation-radicals containing the threonine residue undergo radical-induced dissociations upon collisional activation and photon absorption in the 210-400 nm range. Peptide cation-radicals containing a radical defect at the N-terminal residue, [Ala-Thr-Ala-Arg+H], were generated by electron transfer dissociation (ETD) of peptide dications and characterized by UV-vis photodissociation action spectroscopy combined with time-dependent density functional theory (TD-DFT) calculations of absorption spectra, including thermal vibronic band broadening. The action spectrum of [Ala-Thr-Ala-Arg+H] ions was indicative of the canonical structure of an N-terminally deaminated radical whereas isomeric structures differing in the position of the radical defect and amide bond geometry were excluded.
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