Magacz Marcin, Oszajca Maria, Nawrot-Hadzik Izabela, Drożdż Ryszard, Jurczak Anna, Hadzik Jakub, Smakosz Aleksander, Krzyściak Wirginia
Department of Medical Diagnostics, Faculty of Pharmacy, Jagiellonian University Medical College, Medyczna 9, 30-688 Krakow, Poland.
Doctoral School of Health and Medical Sciences, Jagiellonian University Medical College, 31-008 Krakow, Poland.
Antioxidants (Basel). 2021 Apr 26;10(5):676. doi: 10.3390/antiox10050676.
Lactoperoxidase (LPO) together with its (pseudo)halogenation cycle substrates, HO and thiocyanate ions oxidized to hypothiocyanite ions, form one of the main systems involved in antimicrobial defense within the oral cavity. In bacterial diseases such as dental caries, lactoperoxidase is oxidized to a form known as Compound II, which is characterized by its inability to oxidize SCN, resulting in a decreased generation of antimicrobial products. sp. rizome extracts, due to their high polyphenol content, have been tested as a source of compounds able to regenerate the antimicrobial activity of lactoperoxidase through converting the Compound II to the native LPO state. In the presented study, acetone extracts of , and , together with their five fractions and four selected polyphenols dominating in the studied in extracts, were tested toward lactoperoxidase reactivating potential. For this purpose, IC50, EC50, and activation percentage were determined by Ellman's method. Furthermore, the rate constants for the conversion of Compound I-Compound II and Compound II-native-LPO in the presence of extracts, extracts fractions, and selected polyphenols were determined. Finally, the ability to enhance the antimicrobial properties of the lactoperoxidase system was tested against . We proved that sp. rhizome is the source of lactoperoxidase peroxidation cycle substrates, which can act as activators and inhibitors of the antimicrobial properties of that system. The presented study shows that the reactivation of lactoperoxidase could become a potential therapeutic target in prevention and treatment support in some infectious oral diseases.
乳过氧化物酶(LPO)及其(伪)卤化循环底物,即被氧化为次硫氰酸根离子的过氧化氢(HO)和硫氰酸根离子,构成了口腔内抗菌防御的主要系统之一。在诸如龋齿等细菌性疾病中,乳过氧化物酶被氧化为一种称为化合物II的形式,其特点是无法氧化硫氰酸根,导致抗菌产物的生成减少。由于其高多酚含量,某植物根茎提取物已被测试作为能够通过将化合物II转化为天然LPO状态来恢复乳过氧化物酶抗菌活性的化合物来源。在本研究中,对该植物、另一植物以及第三植物的丙酮提取物及其五个馏分和提取物中占主导地位的四种选定多酚对乳过氧化物酶的再激活潜力进行了测试。为此,采用埃尔曼法测定了半数抑制浓度(IC50)、半数有效浓度(EC50)和激活百分比。此外,还测定了在提取物、提取物馏分和选定多酚存在下化合物I - 化合物II以及化合物II - 天然LPO转化的速率常数。最后,测试了增强乳过氧化物酶系统抗菌性能的能力。我们证明了该植物根茎是乳过氧化物酶过氧化循环底物的来源,其可作为该系统抗菌性能的激活剂和抑制剂。本研究表明,乳过氧化物酶的再激活可能成为某些感染性口腔疾病预防和治疗支持中的一个潜在治疗靶点。