147731-51-9Relevant articles and documents
Investigation of the Effects of Squalene and Squalene Epoxides on the Homeostasis of Coenzyme Q10 in Rats by UPLC-Orbitrap MS
Yu, Wenjing,Sun, Kaiju,Zhang, Liying,Wan, Xilin,Chen, Changbao,Su, Rui,Liu, Yifei,Wang, Hongfeng,Yang, Hongmei
, (2020/08/05)
Squalene has been used as a dietary supplement for a long history due to its potential cancer-preventive function. However, the mechanism has not been investigated in detail yet. Therefore, the aim of this study is to see if the plasma coenzyme Q10 (CoQ10) level will be altered by gavage of squalene and oxidosqualenes to rats. In the present work, a sensitive and simple high-performance analytical method based on ultra-high-performance liquid chromatography coupled with an Orbitrap mass spectrometry (UPLC-Orbitrap-MS) was developed for the quantification of CoQ10 in rat plasma. Coenzyme Q9 (CoQ9) was employed as the internal standard. CoQ10 was determined after acetonitrile-mediated plasma protein precipitation using UPLC-Orbitrap-MS in negative ion mode. Intragastric administration of squalene and the two squalene epoxides into rats once daily for several days elevated the level of CoQ10 in their plasma, but there was no significant difference between high-dose (286 mg/kg) and low-dose (143 mg/kg) groups. Intragastric administration of squalene once a day for 5 consecutive days and oxidosqualenes once a day for 3 consecutive days is necessary for reaching the steady-state level of CoQ10. Our present findings indicate that squalene and oxidosqualenes may be useful for stimulating the synthesis of CoQ10 in rats.
Nanolipid-trehalose conjugates and nano-assemblies as putative autophagy inducers
Colombo, Eleonora,Biocotino, Michele,Frapporti, Giulia,Randazzo, Pietro,Christodoulou, Michael S.,Piccoli, Giovanni,Polito, Laura,Seneci, Pierfausto,Passarella, Daniele
, (2019/09/10)
The disaccharide trehalose is an autophagy inducer, but its pharmacological application is severely limited by its poor pharmacokinetics properties. Thus, trehalose was coupled via suitable spacers with squalene (in 1:2 and 1:1 stoichiometry) and with betulinic acid (1:2 stoichiometry), in order to yield the corresponding nanolipid-trehalose conjugates 1-Sq-mono, 2-Sq-bis and 3-Be-mono. The conjugates were assembled to produce the corresponding nano-assemblies (NAs) Sq-NA1, Sq-NA2 and Be-NA3. The synthetic and assembly protocols are described in detail. The resulting NAs were characterized in terms of loading and structure, and tested in vitro for their capability to induce autophagy. Our results are presented and thoroughly commented upon.
Squalene-Hopene Cyclase: On the Polycyclization Reactions of Squalene Analogues Bearing Ethyl Groups at Positions C-6, C-10, C-15, and C-19
Takahashi, Kazunari,Sasaki, Yusuke,Hoshino, Tsutomu
supporting information, p. 1477 - 1490 (2018/04/06)
Squalene-hopene cyclase (SHC) has been found to convert acyclic squalene into 6,6,6,6,5-fused pentacyclic triterpenes hopene and hopanol. The enzymatic reactions of squalene analogues bearing ethyl groups in lieu of methyl groups at positions C-6, C-10, C-15, and C-19 have been examined to investigate whether the larger ethyl substituents (a C1 unit increment) are accepted as substrates and to investigate how these substitutions affect polycyclization cascades. Analogue 6-ethylsqualene 19a did not cyclize, which indicates that substitution with the bulky group at C-6 completely inhibited the polycyclization reaction. In contrast, 19-ethylsqualene 19b afforded a wide spectrum of cyclization products, including mono-, bi-, tetra-, and pentacyclic products in a ratio of 6:6:1:2. The production of tetra- and pentacyclic scaffolds suggests that the reaction cavity for D-ring formation site is somewhat loosely packed and can accept the 19-ethyl group, and that a robust hydrophobic interaction exists between the 19-ethyl group and the binding site. In contrast to 19b, 10-ethylsqualene 20a and 15-ethylsqualene 20b afforded mainly mono- and bicyclic products, that is, the polycyclization cascade terminated prematurely at the bicyclic reaction stage. Therefore, the catalytic domains for the 10- and 15-methyl binding sites are tightly packed and cannot fully accommodate the Et substituents. The cyclization pathways followed by the ethyl-substituted substrates in the presence of SHC and lanosterol and β-amyrin synthases are compared.
