Department of Natural Sciences, University of Michigan-Dearborn, 4901 Evergreen Rd, Dearborn, MI 48128, USA.
Department of Natural Sciences, University of Michigan-Dearborn, 4901 Evergreen Rd, Dearborn, MI 48128, USA.
Bioorg Med Chem Lett. 2023 Nov 15;96:129529. doi: 10.1016/j.bmcl.2023.129529. Epub 2023 Oct 17.
Riboflavin, a member of the B vitamin family, is a water-soluble vitamin that participates in energy metabolism processes via two coenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), in oxidized and reduced forms. Low levels of riboflavin have been associated with growth and developmental problems. In an effort to investigate the role of hydrogen bonding in the interactions between riboflavin and chicken riboflavin binding protein, the solid state geometry characteristics of a riboflavin derivative stripped of hydroxyl groups except the primary one, N-(6'-hydroxyhexyl)isoalloxazine, were investigated and found that π-stacking and hydrogen bonding involving the isoalloxazine rings are the primary intermolecular interactions. Subsequent comparative fluorescence studies showed that at neutral pH, in presence of the protein, quenching of N-(6'-hydroxyhexyl)isoalloxazine and riboflavin occurred similarly suggesting that the hydroxyl groups were not a key component of the vitamin protein interactions in the binding pocket.
核黄素是维生素 B 族的一员，是一种水溶性维生素，可通过两种辅酶黄素单核苷酸（FMN）和黄素腺嘌呤二核苷酸（FAD）在氧化和还原形式参与能量代谢过程。核黄素水平低与生长和发育问题有关。为了研究氢键在核黄素与鸡核黄素结合蛋白相互作用中的作用，研究了除一个羟基外的羟基被去除的核黄素衍生物，N-（6'-羟基己基）异咯嗪的固态几何特征，发现π-堆积和涉及异咯嗪环的氢键是主要的分子间相互作用。随后的比较荧光研究表明，在中性 pH 值和存在蛋白质的情况下，N-（6'-羟基己基）异咯嗪和核黄素的猝灭相似，这表明羟基不是结合口袋中维生素-蛋白质相互作用的关键组成部分。
