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ARS Home » Plains Area » Grand Forks, North Dakota » Grand Forks Human Nutrition Research Center » Dietary Prevention of Obesity-related Disease Research » Research » Publications at this Location » Publication #107703

Title: BIOLOGICAL BORON INTERACTIONS: CHARGE AND STRUCTURE CHARACTERISTICS REQUIRED FOR BOROESTER FORMATION WITH BIOMOLECULES

Author
item RALSTON, NICHOLAS
item HUNT, CURTISS

Submitted to: Journal of Federation of American Societies for Experimental Biology
Publication Type: Abstract Only
Publication Acceptance Date: 12/10/1999
Publication Date: 3/15/2000
Citation: Ralston, N.V.C., Hunt, C.D. 2000. Biological boron interactions: Charge and structure characteristics required for boroester formation with biomolecules [abstract]. The Federation of American Societies for Experimental Biology Journal. 14:A538.

Interpretive Summary:

Technical Abstract: Boron (B) forms reversible anionic complexes with biomolecules by interacting with vicinal cis diols (VCD) on the ligand. Boroesters stabilized by proximal aromatic groups or cationic moieties should have greater residence times in association with the ligand. Conversely, anionic groups in the proximity of the VCD of the ligand should reduce B association. Capillary electrophoresis (CE) was used to analyze B binding by the cationic biomolecules, S-adenosylmethionine (SAM) and nicotinamide adenine dinucleotide (NAD) in comparison to binding by their structurally related but uncharged forms, adenosine (ADN) and NADH. Uncharged dopamine binding was compared to binding by anionic L-DOPA (carboxylated dopamine). Relative migration times (sample migration time/neutral standard migration time; mT) for SAM, ADN, NAD, NADH, L-DOPA, and dopamine were respectively; 0.927 +/- 0.001, 1.016+/-0.001, 1.352+/-0.004, 1.967+/-0.019, 1.139+/- .002, and 0.704+/-0.001, (mean+/-SD, n=6) as determined by CE (25 kV through 50 cm x 50 um silica capillaries in 200 mM glycyl-glycine (0 mM B) at pH 8.4). When 10 mM B was present in the buffer, change in uT (uT in 10 mM borate/uT in 0 mM borate; delta uT) was greater for the positively charged SAM than for the uncharged ADN (1.043+\-0.001 vs. 1.033+\-0.001, p<0.001). Delta uT for cationic NAD was far greater than the delta uT of the uncharged NADH was (1.083+\-0.001 vs. 1.025+\-0.001, p<0.001). The increase in delta uT in the presence of B for dopamine was the greatest observed while delta uT of the anionic L-DOPA actually decreased (1.169+\- 0.002 vs. 0.973 +\-0.001, p<0.001). Further delineation of the required charge and structure characteristics of biomolecules that interact with B may lead to specific identification of those that require B for function.