Galactose dialdehyde as potential protein cross-linker: proof of principle.
Combined enzymatic oxidation of D-galactose by D-galactose oxidase [EC 1.1.3.9] in water, amination with butylamine, and oxalic acid catalyzed Amadori rearrangement in methanol yielded 1,6-bis(butylamino)-1,6-dideoxy-erythro-hexo-2,5-diulose, demonstrating how in situ formed galacto-hexodialdose can be used to cross-link protein residues. The various species formed during this three-step conversion are present as bicyclic structures in solution as established by 13C labeling and in situ NMR spectroscopy of the reaction mixtures. Using protein (gelatin) instead of butylamine, distinct Amadori product formation was observed using 99% enriched D-(1-(13)C)- and D-(2-(13)C)-galactose.
Schoevaart
Rob
R
Industrial Fermentative Chemistry, Leiden University, Einsteinweg 55, PO Box 9502, NL-2300 RA, Leiden, The Netherlands.
Kieboom
Tom
T
D000447:Aldehydes / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D005690:Galactose / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism; D005692:Galactose Oxidase / Q000378:metabolism; D005780:Gelatin / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D015416:Maillard Reaction; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
D000447:Aldehydes; D003432:Cross-Linking Reagents; D011506:Proteins; D012996:Solutions; C468551:galactose dialdehyde; D005780:Gelatin; D005692:Galactose Oxidase; D005690:Galactose