1160-54-9Relevant articles and documents
Collision-induced dissociative chemical cross-linking reagent for protein structure characterization: Applied Edman chemistry in the gas phase
Dreiocker, Frank,Mueller, Mathias Q.,Sinz, Andrea,Schaefer, Mathias
, p. 178 - 189 (2010)
Chemical cross-linking combined with a subsequent enzymatic digestion andmass spectrometric analysis of the created crosslinked products presents an alternative approach to assess low-resolution protein structures and to gain insight into protein interfaces. In this contribution, we report the design of an innovative cross-linker based on Edman degradation chemistry, which leads to the formation of indicative mass shifted fragment ions and constant neutral losses (CNLs) in electrospray ionization (ESI)-tandem-mass spectrometry (MS/MS) product ion mass spectra, allowing an unambiguous identification of cross-linked peptides. Moreover, the characteristic neutral loss reactions facilitate automated analysis by multiple reaction monitoring suited for high throughput studies with good sensitivity and selectivity. The functioning of the novel cross-linker relies on the presence of a highly nucleophilic sulfur in a thiourea moiety, safeguarding for effective intramolecular attack leading to predictive and preferred cleavage of a glycyl-prolyl amide bond. Our innovative analytical concept and the versatile applicability of the collision-induced dissociative chemical cross-linking reagent are exemplified for substance P, luteinizing hormone releasing hormone LHRH and lysozyme. The novel cross-linker is expected to have a broad range of applications for probing protein tertiary structures and for investigating protein-protein interactions. Copyright
An unusual side reaction of 1-succinimidyl esters during peptide synthesis.
Savrda
, p. 3199 - 3200 (1977)
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Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide
Racys, Daugirdas Tomas,Rea, Dean,Fueloep, Vilmos,Wills, Martin
supporting information; experimental part, p. 4775 - 4782 (2010/08/22)
A new inhibitor, containing a linked proline-piperidine structure, for the enzyme prolyl oligopeptidase (POP) has been synthesised and demonstrated to bind covalently with the enzyme at the active site. This provides evidence that covalent inhibitors of P
Efficient peptide coupling involving sterically hindered amino acids
Katritzky, Alan R.,Todadze, Ekaterina,Angrish, Parul,Draghici, Bogdan
, p. 5794 - 5801 (2008/02/09)
(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)