Nutraceuticals are dietary supplements, utilized to ameliorate health, delay senescence, prevent diseases, and support the proper functioning of the human body. Currently, nutraceuticals are gaining substantial attention due to nutrition and therapeutic potentials. Based on their sources, they are categorized as dietary supplements and herbal bioactive compounds. The global market for nutraceutical is huge i.e. approximately USD 117 billion. Herbal nutraceutical helps in maintaining health and promoting optimal health, longevity, and quality of life. Studies have shown promising results of nutraceuticals to treat several diseases, such as cancer, neurodegenerative diseases, cardiovascular diseases, etc. In the present review, an overview of various bioactive ingredients that act as nutraceuticals (carbohydrates, lipids, edible flowers, alkaloids, medicinal plants, etc.) and their role in health benefits, has been discussed. Further application of nutraceuticals in the prevention of various diseases has also been discussed.

Current Prospects of Nutraceuticals: A Review.

Lactoglobulin is a natural protein present in bovine milk and common component of human diet, known for binding with high affinity wide range of hydrophobic compounds, among them fatty acids 12–20 carbon atoms long. Shorter fatty acids were reported as not binding to β-lactoglobulin. We used X-ray crystallography and fluorescence spectroscopy to show that lactoglobulin binds also 8- and 10-carbon caprylic and capric acids, however with lower affinity. The determined apparent association constant for lactoglobulin complex with caprylic acid is 10.8 ± 1.7 × 103 M−1, while for capric acid is 6.0 ± 0.5 × 103 M−1. In crystal structures determined with resolution 1.9 A the caprylic acid is bound in upper part of central calyx near polar residues located at CD loop, while the capric acid is buried deeper in the calyx bottom and does not interact with polar residues at CD loop. In both structures, water molecule hydrogen-bonded to carboxyl group of fatty acid is observed. Different location of ligands in the binding site indicates that competition between polar and hydrophobic interactions is an important factor determining position of the ligand in β-barrel. Copyright © 2010 John Wiley & Sons, Ltd.

Two modes of fatty acid binding to bovine β-lactoglobulin--crystallographic and spectroscopic studies.

Alkaloids--secrets of life , Alkaloids--secrets of life , کتابخانه دیجیتال جندی شاپور اهواز

Alkaloids--secrets of life

In plant-based food, phenolic compounds usually do not exist in their native form, but as esters, glycosides, or polymers. The native forms, however, require deglycosylation for their intestinal absorption, and aglycone has been considered to be the potential health-protecting/promoting form. The binding of the aglycones of phenolic compounds to bovine and reindeer β-lactoglobulins (βLG) using fluorescence quenching was studied. The effects of pH and storage were also studied. Of the compounds investigated, the majority of flavones, flavonols, flavanones, and isoflavones were bound to βLG. In the pH studies, no significant effects were found. The fact that the phenolic compounds were not released at pH 2 might indicate that they bind to an external part rather than to the central cavity. Studies implicated that βLG could act as a binder or carrier for phenolic compounds in acidic, basic, or neutral conditions and that the ligand/βLG complex can remain stable during storage.

Binding of Phenolic Compounds and Their Derivatives to Bovine and Reindeer β-Lactoglobulin

Structural and thermodynamic studies of binding saturated fatty acids to bovine β-lactoglobulin ☆

The pepper alkaloid piperine is a nontoxic, natural dietary compound with a broad range of physiological activity. The present work is the first demonstration of its interaction with a mammalian protein. Circular dichroism (CD) spectroscopy was used to reveal and analyze the binding of piperine to a lipocalin protein. Induced CD spectra measured in pH 7.7 phosphate buffer at 37 degrees C demonstrated reversible, non-covalent association of piperine with bovine beta-lactoglobulin (BLG), the major whey protein in milk. The binding parameters (K(a) approximately 8 x 10(4) M(-1), n = 0.8) determined from the CD titration data showed no significant differences between the piperine binding properties of the two main genetic variants of BLG (A and B). The vanishing extrinsic CD signal obtained upon acidification of the piperine-BLG sample solution (Tanford transition) suggested that the ligand binds in the central hydrophobic cavity of the beta-barrel. The cavity binding concept was further supported by a CD displacement experiment using palmitic acid, the well-known hydrophobic ligand of BLG. Molecular docking calculations showed that piperine can be efficiently accommodated within the calyx of BLG. Additional molecular modeling calculations indicated that the beta-barrel of human tear lipocalin, human serum retinol binding protein, and human neutrophil gelatinase associated lipocalin might also accommodate a piperine molecule.

Lindsay Sawyer

Papers

Binding of the pepper alkaloid piperine to bovine beta-lactoglobulin: circular dichroism spectroscopy and molecular modeling study.