Determination of antioxidant, DNA protection, enzyme inhibition potential and molecular docking studies of a biomarker ursolic acid in Nepeta species

被引:12
|
作者
Yenigun, Semiha [1 ]
Basar, Yunus [2 ]
Ipek, Yasar [3 ]
Behcet, Lutfi [4 ]
Ozen, Tevfik [1 ]
Demirtas, Ibrahim [2 ,5 ]
机构
[1] Ondokuz Mayis Univ, Fac Sci, Dept Chem, Samsun, Turkiye
[2] Igdir Univ, Fac Arts & Sci, Dept Biochem, Igdir, Turkiye
[3] Cankiri Karatekin Univ, Fac Sci, Dept Chem, Cankiri, Turkiye
[4] Bingol Univ, Fac Arts & Sci, Dept Mol Biol & Genet, Bingol, Turkiye
[5] Ondokuz Mayis Univ, Fac Pharm, Dept Pharmaceut Chem, Samsun, Turkiye
来源
关键词
Nepea species; bioactivity-guided isolation; ursolic acid; bioactivity; molecular docking; OLEANOLIC ACID; MYCOBACTERIUM-TUBERCULOSIS; ALPHA-GLUCOSIDASE; IN-VITRO; CONSTITUENTS; EXTRACTS; L; ACETYLCHOLINESTERASE; TRITERPENES; POLYPHENOLS;
D O I
10.1080/07391102.2023.2229440
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ursolic acid (UA), which has many biological properties such as anti-cancer, anti-inflammatory and antioxidant, and regulates some pharmacological processes, has been isolated from the flowers, leaves, berries and fruits of many plant species. In this work, UA was purified from the methanol-chloroform crude extract of Nepeta species (N. aristata, N. baytopii, N. italica, N. trachonitica, N. stenantha) using a silica gel column with chloroform or ethyl acetate solvents via bioactivity-guided isolation. The most active sub-fractions were determined under bioactivities using antioxidant and DNA protection activities and enzyme inhibitions. UA was purified from these fractions and its structure was elucidated by NMR spectroscopy techniques. The highest amount of UA was found in N. stenantha (8.53 mg UA/g), while the lowest amount of UA was found in N. trachonitica (1.92 mg UA/g). The bioactivities of UA were evaluated with antioxidant and DNA protection activities, enzyme inhibitions, kinetics and interactions. The inhibition values (IC50) of & alpha;-amylase, & alpha;-glucosidase, urease, CA, tyrosinase, lipase, AChE, and BChE were determined between 5.08 and 181.96 & mu;M. In contrast, K-i values of enzyme inhibition kinetics were observed between 0.04 and 0.20 mM. In addition, K-i values of these enzymes for enzyme-UA interactions were calculated as 0.38, 0.86, 0.45, 1.01, 0.23, 0.41, 0.01 and 2.24 & mu;M, respectively. It is supported that UA can be widely used as a good antioxidant against oxidative damage, an effective DNA protector against genetic diseases, and a suitable inhibitor for metabolizing enzymes.Communicated by Ramaswamy H. Sarma
引用
收藏
页码:5799 / 5816
页数:18
相关论文
共 42 条