Solid-state 13C-NMR spectroscopy of adduction products of 2,5-hexanedione with ribonuclease, albumin, and rat neurofilament protein.
The Paal-Knorr condensation reaction between the gamma-diketone 2,5-hexanedione (2,5-HD) and epsilon-amine moieties of proteins of various molecular weight, including ribonuclease (RNase), bovine serum albumin (BSA) and rat neurofilament (NF), has been investigated by solid-state 13C-NMR spectroscopy. These proteins all reacted with 2,5-HD with the formation of 2,5-dimethylpyrrole (2,5-DMP) derivatives. The size and complexity of the protein affected the rate of formation of 2,5-DMP derivatives. Using the selective reducing reagent NaCNBH3, the Paal-Knorr reaction intermediates were trapped by conversion into amines, which were identified by solid-state NMR spectroscopy. The secondary autoxidation reaction following the formation of 2,5-DMP derivatives was also studied by solid-state NMR spectroscopy.
Yan
B
B
Department of Chemistry, University at Albany, State University of New York 12222, USA.
DeCaprio
A P
AP
Zhu
M
M
Bank
S
S
D000818:Animals; D002247:Carbon Isotopes; D018736:DNA Adducts / Q000378:metabolism; D006588:Hexanones / Q000378:metabolism*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D016900:Neurofilament Proteins / Q000378:metabolism*; D011758:Pyrroles / Q000378:metabolism; D051381:Rats; D012260:Ribonucleases / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D002247:Carbon Isotopes; D018736:DNA Adducts; D006588:Hexanones; D016900:Neurofilament Proteins; D011758:Pyrroles; D012710:Serum Albumin, Bovine; C011269:2,5-hexanedione; D012260:Ribonucleases