China
Africa
Explore chapters and articles related to this topic
Herbs with Antidepressant Effects
Published in Scott Mendelson, Herbal Treatment of Major Depression, 2019
Hedyosmum brasiliense is a South American plant native to the Atlantic forest region. Its peppermint-like flavor is prized, and it is a popular beverage in Brazil and Bolivia. It is commonly known as “cidrão” or “Cha De Soldado,” and in folk medicine this aromatic species is widely used as a calmative, tranquilizer, and hypnotic. Among the phytochemicals contained in Hedyosmum brasiliense are α-terpineol, curzerene, pinocarvone, β-thujene, podoandin, 1,2-epoxy-10α-hydroxy-podoandin, 1-hydroxy-10,15-methylenepodoandin, 15-acetoxy-isogermafurenolide, 8α/β,9α-hydroxy-onoseriolide, guaianolide podoandin, onoseriolide, scopoletin, vanillin, vanillic acid, protocatechuic aldehyde, and ethyl caffeate.1,2
Cocoyam (Colocasia esculenta) modulates some parameters of testosterone propionate-induced rat model of benign prostatic hyperplasia
Published in Drug and Chemical Toxicology, 2022
Kate Eleazu, Patrick Maduabuchi Aja, Chinedum Ogbonnaya Eleazu
Benzoic acid, gallic, protocatechuic acids, cinnamic acid, p-coumaric, ferulic, vanillic, catechin, caffeic, salicyclic, homogentisic, homovanillic, pyrogallic, syringic, mandelic, M-OH benzoic, p-hydroxy benzoic, cyanidin-3-O-glucoside, cyanidin coumaroyl, aesculetin, ethyl caffeate and tannic acids, have been reported to possess beneficial effects such as: antioxidants, anti-inflammatory, and anti-proliferating properties (Kampa et al.2004, Prasanthi et al.2017, Akanni et al.2020).
Natural compounds as inhibitors of transthyretin amyloidosis and neuroprotective agents: analysis of structural data for future drug design
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Lidia Ciccone, Nicoló Tonali, Susanna Nencetti, Elisabetta Orlandini
The crystal structures of caffeic acid, NDGA, and their derivatives, in complex with TTR V30M, were solved (4QRF, 4PWF, 4PWG, 4PWH, 4PWI, 4PWK, and 4PWJ, Table 1)56. The r.m.s.d. value calculated on Cα atoms between apo-V30M and V30M-compound complexes was in range from 0.30 to 0.56 Å, therefore, the ligand interaction with the T4-BS does not induced relevant structural differences. Regarding the caffeic acid derivatives, the catechol moieties of CAPE (4QRF), CA alkyl acids (4PWG and 4PWH), and the guaiacol function were located into the inner subsites, while the alkyl ether groups point towards the outer BS (Figure 11(A)). The oxycarbonyl and alkyl moieties of CA ethyl esters (ethyl caffeate and 1,1-dimethylallyl caffeate) are stabilised by hydrophobic interaction with amino acid side chain Lys15, Leu17, Thr106, Ala108, and Val121. Rosmarinic acid (4PWI) binds to TTR displacing similar orientation with one catechol function placed into the inner BS and the other pointing towards the outer cavity (Figure 11(B)). Rosmarinic acid interacts with TTR keeping the same interactions of the other CAPE and CA derivatives and in addition its carboxylic moiety makes salts bridge with Lys15 increasing the complex stability. The binding mode described for caffeic acid derivatives is analogue to that of NDGA (4PWJ) and its derivative dihydroguaiaretic acid (4PWK) (Figure 11(C)): one catechol group is located into the inner cavity and the other points towards the outer subsite, while the hydrophobic linker is contorted by a-polar side chain of Lys15, Leu17, Thr106, Ala108, and Val121. It is interesting to underline that only the dihydroguaiaretic acid derivative binds to the two TTR subunits in asymmetric way leading to the loss of the HB with Ser117 in the dimer BB’. As observed above, the 3-OCH3 of NDGA resulted as the most effective functional group for the inhibitory activity. The methoxy group is in fact, involved in hydrophobic interactions with Ala108, Leu110, Ser117, and Thr119 and hydrogen-bonded with Ser117. This observation confirms the importance of hydrophobicity to well interact with the inner cavity of the binding pocket and the necessity of HB donor/acceptor groups for the interaction with Ser117. A two-aromatic-ring substructure having a linker connecting them, such as biphenyl, stilbene, and biphenyl ether, seems to be a good template for the design of TTR amyloid fibril inhibitors. The linker length should be sufficient to enable the inhibitor to interact with the outer binding pocket, where other hydrophobic interactions with Thr106 and Val121 are necessary for a better affinity, and to reach the Lys15 for establish a salt bridge.