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Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Among more than 300 amino acids in nature, only 20 of them serve as building blocks of protein in plants, animals, and humans (38–39). The names of 20 α-amino acids present in proteins are: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine (37–39). Their general chemical structure is the following.
Marine Fungi-Derived Secondary Metabolites: Potential as Future Drugs for Health Care
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Syed Shams Ul Hassan, Hui-Zi Jin, Abdur Rauf, Saud Bawazeer, Hafiz Ansar Rasul Suleria
Current articles were reviewed for marine sources of secondary metabolites for health care. Currently, thousands of compounds with their unique chemical structures and with their bioactivities have been reported from marine fungi. The development of these biomolecules can overcome the problems owing to the early entrance of first marine natural products in drug market [3]. Can a resolute channel of marine drugs be provided by an ocean? The chemical structure can be analyzed by various emerging techniques, such as sampling strategies [45], modern culturing technique [13], genetic engineering, and nanoscale NMR [14].
Components of Nutrition
Published in Christopher Cumo, Ancestral Diets and Nutrition, 2020
Yet pessimism and circumspection are unnecessary in all cases. The subject of ongoing research, beneficial phytochemicals appear to be numerous in vegetables, fruits, legumes, and whole grains. Phytochemicals may be conspicuous, giving carrots, tomatoes, and other vegetables and fruits their distinctive appearance and enhancing aroma and flavor in onions, leeks (Allium ampeloprasum), garlic (A. sativum), chives (A. schoenoprasum), kurrat or wild leek (A. ampeloprasum), and shallots (A. cepa). Chemical structure shapes attributes and functions.
Synthesis and evaluation of a large library of nitroxoline derivatives as pancreatic cancer antiproliferative agents
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Serena Veschi, Simone Carradori, Laura De Lellis, Rosalba Florio, Davide Brocco, Daniela Secci, Paolo Guglielmi, Mattia Spano, Anatoly P. Sobolev, Alessandro Cama
For these reasons, nitroxoline structure has prompted the Medicinal chemists to explore the structural requirements suitable to improve antitumor effects. In previous papers, taking advantage of the reactivity of the quinoline nucleus, most authors studied the introduction of halogens and additional side chains as well as modifications of the nitro group17,18. A limitation of most previous efforts was that they were directed towards the cathepsin B inhibitory activity, disregarding the other mechanisms of action demonstrated for nitroxoline as an anticancer compound so far. The aim of our study was the hitherto unexplored modification of the OH group. This could lead to a strong alteration of the chemical–physical characteristics of this 8-hydroxyquinoline. Indeed, this functional group endowed the chemical structure with a discrete acidity (reinforced by the p-NO2 moiety) and chelating ability. Furthermore, this phenolic compound is characterised by proton and electron-donating capacity and, as a consequence, antioxidant properties which can occur during several important biological processes19.
Not the comfy chair! Cancer drugs that act against multiple active sites
Published in Expert Opinion on Therapeutic Targets, 2019
Laurence Booth, Andrew Poklepovic, Paul Dent
Differences in chemical structure do not influence inhibition of the primary target but can profoundly influence drug actions on the other, ‘unknown’ targets. Neratinib and afatinib despite having quite different chemical structures both were developed as irreversible, i.e. suicide, inhibitors of ERBB1, ERBB2, and ERBB4 [34,35]. They both block homo- and hetero-phosphorylation. Tyrosine phosphorylated ERBB family receptors act to causes downstream signaling through the ERK1/2, ERK5, JNK1/2, PI3K, STAT3, and NFĸB pathways [36,37]. Several publications using neratinib and afatinib have presented evidence that these kinase inhibitors not only prevent receptor tyrosine phosphorylation but can also act to promote receptor internalization and degradation [38–40]. Two groups demonstrated that whereas the ERBB1/2/4 inhibitor lapatinib can enhance ERBB2 expression, neratinib decreased ERBB2 levels [41–43]. In SKOV3 breast cancer cells, low concentrations of neratinib could suppress endogenous and over-expressed wild type ERBB2 levels within four hours [44]. Others have suggested neratinib could decrease ERBB1 expression or down-regulate ERBB2 via ubiquitination and endocytic degradation [45–48]. Thus, over the past 10 years many groups have presented consistent evidence that suicide ERBB1/2/4 inhibitors can act as kinase inhibitors and also cause ERBB receptor degradation.
Binding site comparisons for target-centered drug discovery
Published in Expert Opinion on Drug Discovery, 2019
For some five decades, drug design has been based on matching a chemical structure with a specific binding site in a protein. Comparison of binding sites, a relatively new approach to drug development, inverts this problem and allows searching for binding sites in any protein that match a given chemical structure. The binding site comparison approach comprises various computer methods that enable the detection of similarities between proteins irrespective of sequence and fold similarities [1–12]. These methods are based on the fact that binding sites on proteins are more evolutionarily conserved than the rest of the protein structure. Common to the methods is that they compare structures of two binding sites with each other at one time, resulting in a computed degree of similarity of the two compared binding sites and in their three-dimensional superimposition. Pre-knowledge of one or both binding sites is not necessary; some methods compare the selected binding site against the entire protein structure [1,5], and some compare whole proteins against whole proteins [2,3]. Unlike global comparisons that compare protein backbones, these methods allow one to find locally restricted similar interactions and structural patterns in proteins that are most often present within drug binding sites.