Anti‑diabetic effect of the lupinalbin A compound isolated from <em>Apios americana</em>: <em>In vitro</em> analysis and molecular docking study

Kim,Hyo-Young; Kim,Jang Hoon; Jeong,Hye Gwang; Jin,Chang Hyun

doi:10.3892/br.2021.1415

Anti‑diabetic effect of the lupinalbin A compound isolated from Apios americana: In vitro analysis and molecular docking study

Authors:
- Hyo-Young Kim
- Jang Hoon Kim
- Hye Gwang Jeong
- Chang Hyun Jin
View Affiliations

Affiliations: Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup‑si, Jeollabuk‑do 56212, Republic of Korea, College of Pharmacy, Chungnam National University, Daejeon, Chungcheongnam‑do 34134, Republic of Korea
Published online on: February 26, 2021 https://doi.org/10.3892/br.2021.1415
Article Number: 39
Copyright: © Kim et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

Metrics: Total Views: 0 (Spandidos Publications: | PMC Statistics: )

Metrics: Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )

Cited By (CrossRef): 0 citations Loading Articles...

Abstract

Dipeptidyl peptidase 4 (DPP4) and α‑glucosidase inhibitors have been developed as anti‑diabetic agents for the treatment of diabetes mellitus. In the present study, the anti‑diabetic effects of the lupinalbin A compound isolated from Apios americana was investigated by measuring its inhibitory activity against DPP4 and α‑glucosidase. To detect the inhibitory effect of lupinalbin A, DPP4 and α‑glucosidase assays were performed in vitro. Molecular docking analysis was performed using AutoDock 4.2. The IC₅₀ values of lupinalbin A against DPP4 and α‑glucosidase were 45.2 and 53.4 µM, respectively. Analysis of the enzyme kinetics revealed that lupinalbin A interacted with the active site of DPP4 in a competitive manner, with an inhibition constant (Ki) value of 35.1±2.0 µM, whereas the lupinalbin A interaction with α‑glucosidase was non‑competitive, with a Ki value of 45.0 µM. Molecular docking analysis revealed a binding pose between the DPP4 enzyme and lupinalbin A. Taken together, these data suggest lupinalbin A is more effective against DPP4 than α‑glucosidase, with regard to its anti‑diabetic effects.

View Figures

View References

1	Wild S, Roglic G, Green A, Sicree R and King H: Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care. 27:1047–1053. 2004.PubMed/NCBI View Article : Google Scholar
2	Kim SM, Lee JS, Lee J, Na JK, Han JH, Yoon DK, Baik SH, Choi DS and Choi KM: Prevalence of diabetes and impaired fasting glucose in Korea: Korean National Health and Nutrition Survey 2001. Diabetes Care. 29:226–231. 2006.PubMed/NCBI View Article : Google Scholar
3	DeFronzo RA: Pathogenesis of type 2 diabetes mellitus. Med Clin North Am. 88:787–835, ix. 2004.PubMed/NCBI View Article : Google Scholar
4	Zhao BT, Le DD, Nguyen PH, Ali MY, Choi JS, Min BS, Shin HM, Rhee HI and Woo MH: PTP1B, α-glucosidase, and DPP-IV inhibitory effects for chromene derivatives from the leaves of Smilax china L. Chem Biol Interact. 253:27–37. 2016.PubMed/NCBI View Article : Google Scholar
5	Li ZP, Song YH, Uddin Z, Wang Y and Park KH: Inhibition of protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase by xanthones from Cratoxylum cochinchinense, and their kinetic characterization. Bioorg Med Chem. 26:737–746. 2018.PubMed/NCBI View Article : Google Scholar
6	Yazbeck R, Howarth GS and Abbott CA: Dipeptidyl peptidase inhibitors, an emerging drug class for inflammatory disease? Trends Pharmacol Sci. 30:600–607. 2009.PubMed/NCBI View Article : Google Scholar
7	Hopsu-Havu VK and Glenner GG: A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide. Histochemie. 7:197–201. 1966.PubMed/NCBI View Article : Google Scholar
8	Gorrell MD, Gysbers V and McCaughan GW: CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes. Scand J Immunol. 54:249–264. 2001.PubMed/NCBI View Article : Google Scholar
9	Morimoto C and Schlossman SF: The structure and function of CD26 in the T-cell immune response. Immunol Rev. 161:55–70. 1998.PubMed/NCBI View Article : Google Scholar
10	Drucker DJ: Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes: Preclinical biology and mechanisms of action. Diabetes Care. 30:1335–1343. 2007.PubMed/NCBI View Article : Google Scholar
11	Mulvihill EE and Drucker DJ: Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors. Endocr Rev. 35:992–1019. 2014.PubMed/NCBI View Article : Google Scholar
12	Wilson PW, Pichardo FJ, Liuzzo JA, Blackmon WJ and Reynolds BD: Amino acids in the american groundnut (Apios americana). J Food Sci. 52:224–225. 1987.
13	Ichige M, Fukuda E, Miida S, Hattan J, Misawa N, Saito S, Fujimaki T, Imoto M and Shindo K: Novel isoflavone glucosides in groundnut (Apios americana Medik) and their antiandrogenic activities. J Agric Food Chem. 61:2183–2187. 2013.PubMed/NCBI View Article : Google Scholar
14	Kaneta H, Koda M, Saito S, Imoto M, Kawada M, Yamazaki Y, Momose I and Shindo K: Biological activities of unique isoflavones prepared from Apios americana Medik. Biosci Biotechnol Biochem. 80:774–778. 2016.PubMed/NCBI View Article : Google Scholar
15	Kim JH, Kim HY, Kang SY, Kim YH and Jin CH: Soluble epoxide hydrolase inhibitory activity of components isolated from Apios americana Medik. Molecules. 22(1432)2017.PubMed/NCBI View Article : Google Scholar
16	Kim JH, Kim HY, Kang SY, Kim JB, Kim YH and Jin CH: Chemical constituents from Apios americana and their inhibitory activity on tyrosinase. Molecules. 23(232)2018.PubMed/NCBI View Article : Google Scholar
17	Iwai K and Matsue H: Ingestion of Apios americana Medikus tuber suppresses blood pressure and improves plasma lipids in spontaneously hypertensive rats. Nutr Res. 27:218–224. 2007.
18	Gilbert ER and Liu D: Anti-diabetic functions of soy isoflavone genistein: Mechanisms underlying its effects on pancreatic β-cell function. Food Funct. 4:200–212. 2013.PubMed/NCBI View Article : Google Scholar
19	Kim HY, Kim JH, So Y, Kang SY, Jeong HG and Jin CH: Anti-inflammatory effect of lupinalbin A isolated from Apios americana on lipopolysaccharide-treated RAW264.7 cells. Molecules. 23(583)2018.PubMed/NCBI View Article : Google Scholar
20	Bai Y, Xu Y, Chang J, Wang X, Zhao Y and Yu Z: Bioactives from stems and leaves of mung beans (Vigna radiata L.). J Funct Foods. 25:314–322. 2016.
21	Yang D, Xie H, Jiang Y and Wei X: Phenolics from strawberry cv. Falandi and their antioxidant and α-glucosidase inhibitory activities. Food Chem. 194:857–863. 2016.PubMed/NCBI View Article : Google Scholar
22	Kim JH, Ryu YB, Lee WS and Kim YH: Neuraminidase inhibitory activities of quaternary isoquinoline alkaloids from Corydalis turtschaninovii rhizome. Bioorg Med Chem. 22:6047–6052. 2014.PubMed/NCBI View Article : Google Scholar
23	Meng XY, Zhang HX, Mezei M and Cui M: Molecular docking: A powerful approach for structure-based drug discovery. Curr Comput Aided Drug Des. 7:146–157. 2011.PubMed/NCBI View Article : Google Scholar
24	de Ruyck J, Brysbaert G, Blossey R and Lensink MF: Molecular docking as a popular tool in drug design, an in silico travel. Adv Appl Bioinform Chem. 9:1–11. 2016.PubMed/NCBI View Article : Google Scholar
25	Heitz MP and Rupp JW: Determining mushroom tyrosinase inhibition by imidazolium ionic liquids: A spectroscopic and molecular docking study. Int J Biol Macromol. 107 (Pt B):1971–1981. 2018.PubMed/NCBI View Article : Google Scholar
26	Seong SH, Ali MY, Kim HR, Jung HA and Choi JS: BACE1 inhibitory activity and molecular docking analysis of meroterpenoids from Sargassum serratifolium. Bioorg Med Chem. 25:3964–3970. 2017.PubMed/NCBI View Article : Google Scholar
27	Fan J, Johnson MH, Lila MA, Yousef G and de Mejia EG: Berry and citrus phenolic compounds inhibit dipeptidyl peptidase IV: Implications in diabetes management. Evid Based Complement Alternat Med. 2013(479505)2013.PubMed/NCBI View Article : Google Scholar