Mangiferin: a review of dietary sources, absorption, metabolism, bioavailability, and safety.

Mangiferin is a potential candidate for use in nutraceutical and functional food applications due to its numerous bioactivities. However, the low bioavailability of mangiferin is a major limitation for establishing efficacy for use. This review describes current information on known food sources and factors that influence mangiferin contents, absorption, and metabolism features, and recent progress that has come from research efforts to increase the bioavailability of mangiferin. We also list patents that targeted to enhance mangiferin bioavailability. Mangifera indica L. is the major dietary source for mangiferin, a xanthone that varies widely in different parts of the plant and is influenced by many factors that involve plant propagation and post-harvest processing. Mangiferin absorption occurs mostly in the small intestine by passive diffusion with varying absorption capacities in different segments of the gastrointestinal tract. Recent research has led to the development of novel technologies to encapsulate mangiferin in nano/microparticle carrier systems as well as generate mangiferin derivatives to improve solubility and bioavailability. Preclinical studies reported that mangiferin < 2000 mg/kg is generally nontoxic. The safety and the increase in bioavailability are key limiting factors for developing successful applications for mangiferin as a nutritional dietary supplement or nutraceutical.Supplemental data for this article is available online at.

Investigation into the site-specific binding interactions between chlorogenic acid and ovalbumin using multi-spectroscopic and in silico simulation studies.

The binding interactions of bioactive compounds with proteins are of great importance in the food, biochemistry and pharmaceutical fields. Herein, the binding mechanisms between 5-O-caffeoylquinic acid (5-CQA) and ovalbumin (OVA) were investigated by multi-spectroscopic studies combined with docking and molecular dynamics (MD) simulations. The emission intensity of OVA was quenched by 5-CQA and Stern-Volmer analysis indicated the existence of a static suppression by OVA-5-CQA complex formation. Thermodynamic parameters revealed that the formation of complex was spontaneously driven by electrostatic and hydrogen-bonding interactions. Circle dichroism analyses showed that 5-CQA decreased the α-helix content of OVA structure from 58.05% to 54.32% upon increased OVA:5-CQA ratio to 1:3. Molecular docking results suggested 5-CQA forms hydrogen bond interactions with N88, T91, K92, N94, S98, F99, S100 and L101 residues of OVA. The experimental values were in good agreement with the calculated binding free energy values obtained by MD simulation (R2 = 0.89).Communicated by Ramaswamy H. Sarma.