Phytochemical and Bioactivity Analysis of Several Methanolic Extracts of Nine Bryophytes Species

Bryophytes are a class of organisms found all over the globe except the sea. They can grow on different surfaces and are known for their fragrant aromas and strong hot and bitter taste. Bryophytes have been used in traditional Chinese medicine for the treatment of many pathological conditions. In the current study, we describe the bioactivities present in methanolic extracts obtained from 9 species of bryophytes. Plant samples were dried and extracted in a water/methanol solution which was explored for flavonoid and phenolic content. Afterwards, the extracts were analyzed for their potential bioactivities including DPP4 inhibition, metal chelation, antioxidant, and antiglycation activities. Results indicate that the methanolic extracts of each species showed high effectiveness for different bioactivities. The current findings suggest these bryophytes as promising source of therapeutics against oxidative stress, hypertension, and diabetes.

Keywords:

Bryophytes bioactive molecules, diabetes, antiglycation, DPP-4,

PDF

___

1. Apak, R., Guclu, K., Ozyurek, M., Karademir, S. E., & Altun, M. (2005). Total antioxidant capacity assay of human serum using copper(II)-neocuproine as chromogenic oxidant: The CUPRAC method. Free Radical Research, 39(9), 949–961. https://doi.org/10.1080/10715 76050 0210145
2. Singleton, V. L., Orthofer, R., & Lamuela-Raventós, R. M. (1998). Analysis of total phenols and other oxidation substrates and antioxidants by means of folin-ciocalteu reagent. Methods in Enzymology, 299, 152–178
3. Arvouet-Grand A, Vennat B, Pourrat A, Legret P. Standardisation d'un extrait de propolis et identification des principaux constituants [Standardization of propolis extract and identification of principal constituents]. J Pharm Belg. 1994 Nov-Dec;49(6):462-8. French. PMID: 7884635.
4. Zeytunluoglu, A., & Zihnioglu, F. (2015). Evaluation of some plants for potential dipeptidyl peptidase IV inhibitory effects in vitro. Turkish Journal of Biochemistry-Turk Biyokimya Dergisi, 40(3), 217–223. https://doi.org/10.1515/tjb.2015.0004
5. T. Matsui, C. Yoshimoto, K. Osajima, T. Oki, Y. Osajima In vitro survey of α-glucosidase inhibitory food components Bioscience, Biotechnology and Biochemistry, 60 (1996), pp. 2019-2022
6. Forbes, J. M., & Fotheringham, A. K. (2017). Vascular complications in diabetes: old messages, new thoughts. Diabetologia, 60(11), 2129-2138. https://doi.org/10.1007/s00125-017-4360-x
7. Cho, N., Shaw, J. E., Karuranga, S., Huang, Y., da Rocha Fernandes, J. D., Ohlrogge, A. W., & Malanda, B. (2018). IDF Diabetes Atlas: Global estimates of diabetes prevalence for 2017 and projections for 2045. Diabetes research and clinical practice, 138, 271-281. https://doi.org/10.1016/j.diabres.2018.02.023
8. Kajaria, D., Ranjana, J. T., Tripathi, Y. B., & Tiwari, S. (2013). In-vitro α amylase and glycosidase inhibitory effect of ethanolic extract of antiasthmatic drug—Shirishadi. Journal of advanced pharmaceutical technology & research, 4(4), 206.
9. Wang, X., Cao, J., Dai, X., Xiao, J., Wu, Y., & Wang, Q. (2017). Total flavonoid concentrations of bryophytes from Tianmu Mountain, Zhejiang Province (China): Phylogeny and ecological factors. PloS one, 12(3), e0173003.
10. ASLANBABA, B., YILMAZ, S., YAYINTAŞ, Ö. T., ÖZYURT, D., & ÖZTÜRK, B. D. (2017). Total phenol content and antioxidant activity of mosses from Yenice forest (Ida mountain). Journal of Scientific Perspectives, 1(1), 1-12.
11. Sethi, S., Joshi, A., Arora, B., Bhowmik, A., Sharma, R. R., & Kumar, P. (2020). Significance of FRAP, DPPH, and CUPRAC assays for antioxidant activity determination in apple fruit extracts. European Food Research and Technology, 246(3), 591-598.
12. McCue, P., Kwon, Y.I., Shetty, K., 2005, Anti-diabetic and anti-hypertensive potential of sprouted and solid-state bioprocessed soybean, Asia Pac J Clin Nutr., 14(2), 145-52.
13. Rahim, F., Zaman, K., Taha, M., Ullah, H., Ghufran, M., Wadood, A., ... & Nawaz, F. (2020). Synthesis, in vitro alpha-glucosidase inhibitory potential of benzimidazole bearing bis-Schiff bases and their molecular docking study. Bioorganic chemistry, 94, 103394.
14. Xiong, Y., Ng, K., Zhang, P., Warner, R. D., Shen, S., Tang, H. Y., ... & Fang, Z. (2020). In Vitro α-Glucosidase and α-Amylase Inhibitory Activities of Free and Bound Phenolic Extracts from the Bran and Kernel Fractions of Five Sorghum Grain Genotypes. Foods, 9(9), 1301.
15. Peng, C.-H., Yang, Y.-S., Chan, K.-C., Wang, C.-J., Chen, M.-L., Huang, C.-N., et al. (2014). Hibiscus sabdariffa polyphenols alleviate insulin resistance and renal epithelial to mesenchymal transition: a novel action mechanism mediated by type 4 dipeptidyl peptidase. J. Agric. Food Chem. 62, 9736–9743. doi: 10.1021/ jf5024092
16. Kalhotra P, Chittepu VCSR, Osorio-Revilla G, Gallardo-Velazquez T. Phytochemicals in Garlic Extract Inhibit Therapeutic Enzyme DPP-4 and Induce Skeletal Muscle Cell Proliferation: A Possible Mechanism of Action to Benefit the Treatment of Diabetes Mellitus. Biomolecules. 2020 Feb 14;10(2):305. doi: 10.3390/biom10020305. PMID: 32075130; PMCID: PMC7072494.
17. Zakłos-Szyda, M., Kowalska-Baron, A., Pietrzyk, N., Drzazga, A., & Podsędek, A. (2020). Evaluation of Viburnum opulus L. Fruit Phenolics Cytoprotective Potential on Insulinoma MIN6 Cells Relevant for Diabetes Mellitus and Obesity. Antioxidants (Basel, Switzerland), 9(5), 433. https://doi.org/10.3390/antiox9050433
18. Fan J, Johnson MH, Lila MA, Yousef G, de Mejia EG. Berry and Citrus Phenolic Compounds Inhibit Dipeptidyl Peptidase IV: Implications in Diabetes Management. Evid Based Complement Alternat Med. 2013;2013:479505. doi: 10.1155/2013/479505. Epub 2013 Aug 29. PMID: 24069048; PMCID: PMC3773436.
19. Ansari, N. A., & Rasheed, Z. (2009). Non-enzymatic glycation of proteins: From diabetes to cancer. Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 3(4), 335–342. https://doi.org/10.1134/s1990 75080 9040027
20. Sattarahmady, N., Moosavi-Movahedi, A. A., Ahmad, F., Hakimelahi, G. H., Habibi-Rezaei, M., Saboury, A. A., & Sheibani, N. (2007). Formation of the molten globule-like state during prolonged glycation of human serum albumin. Biochimica et Biophysica Acta (BBA)-General Subjects, 1770(6), 933-942.
21. Christen, Y. (2000). Oxidative stress and Alzheimer disease. The American journal of clinical nutrition, 71(2), 621S-629S
22. Decker, E. L., & Reski, R. (2020). Mosses in biotechnology. Current opinion in biotechnology, 61, 21-27.
23. Li, X., Wang, X., Chen, D., & Chen, S. (2011). Antioxidant activity and mechanism of protocatechuic acid in vitro. Functional Foods in Health and Disease, 1(7), 232. https://doi.org/10.31989/ ffhd.v1i7.127
24. Kani, H. K., Kocazorbaz, E. K., & Zihnioglu, F. (2019). Investigation and isolation of peptide based antiglycating agents from various sources. Turkish Journal of Biochemistry, 44(5), 699-705.
25. Duez, H., Cariou, B., & Staels, B. (2012). DPP-4 inhibitors in the treatment of type 2 diabetes. Biochemical pharmacology, 83(7), 823-832.
26. Dukic-Stefanovic, S., Schinzel, R., Riederer, P., & Münch, G. (2001). AGES in brain ageing: AGE-inhibitors as neuroprotective and anti-dementia drugs?. Biogerontology, 2(1), 19-34.
27. Nawale, R. B., Mourya, V. K., & Bhise, S. B. (2006). Non-enzymatic glycation of proteins: a cause for complications in diabetes.