Solid-state 13C-NMR spectroscopy of adduction products of 2,5-hexanedione with ribonuclease, albumin, and rat neurofilament protein.
Related Articles Solid-state 13C-NMR spectroscopy of adduction products of 2,5-hexanedione with ribonuclease, albumin, and rat neurofilament protein.
Chem Biol Interact. 1996 Oct 21;102(2):101-16
Authors: Yan B, DeCaprio AP, Zhu M, Bank S
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.
PMID: 8950225 [PubMed - indexed for MEDLINE]
Source:
PubMed