Isolation of Human Renin Inhibitor from Soybean: Soyasaponin I Is the Novel Human Renin Inhibitor in Soybean

We found human renin inhibitory activity in soybean and isolated the active compound, soybean renin inhibitor (SRI). The physico-chemical data on the isolated SRI were identical with those of soyasaponin I. SRI showed significant inhibition against recombinant human renin, with an IC₅₀ value of 30 μg/ml. Kinetic studies with SRI indicated partial noncompetitive inhibition, with a K_i value of 37.5 μM. On the other hand, SRI weakly inhibited pepsin, papain, and bromeline activities, but did not inhibit other proteinases, such as trypsin, kallikrein, angiotensin converting enzyme, and aminopeptidase M. Moreover, a significant (p<0.05) decrease in the systolic blood pressure of spontaneously hypertensive rats was observed when partially purified SRI was orally administrated at 40 mg/kg/d for 7 weeks. This is the first demonstration of a renin inhibitor from soybean, soyasaponin I.     

Superoxide- and 1,1-Diphenyl-2-picrylhydrazyl Radical-scavenging Activities of Soyasaponin β g Related to Gallic Acid

Soyasaponin β g at 1 mM had 8% scavenging activity for O₂ ^-, and 25 μM β scavenged 20.9% for the DPPH radical (IC₅₀: 63.8 μM). In the soyasaponin β g-gallic acid system, synerigistic effects were observed at a low level of gallic acid concentration. The spin density distribution calculated by the MNDO/AM1 method showed unpaired electron localization on the carbons at C-4 and C-6, and on the ketone group at C-4 of the DDMP moiety. Furthermore, for soyasaponin β g, the MNDO/AM1 method gave an ionization potential of 8.38 eV, electron affinity of 1.16 eV and Mulliken electronegativity of 4.77 eV. Based on this evidence, the synergistic antiradical effects of the soyasaponin β g-gallic acid system are assumed to involve two-electron reduction from gallic acid.     

大豆皂甙抗癌活性研究进展

本文就大豆皂甙的抗癌活性研究进展进行概述,并对未来研究方向进行了展望.     

The Structures of Water-soluble Polysaccharides Isolated from Bamboo Shoot

The structures of two polysaccharides reported in the previous paper were studied by means of methylation analysis and the Smith degradation. As a result, it was concluded that the water-soluble xylan consisted essentially of a (l→4)-linked β-d-xylopyranosyl chain and contained l-arabinofuranosyl residues linked through the C–l as terminal side units. Unambiguous information concerning the residues of d-glactose and d-glucuronic acid as the constituents of the xylan has not been obtained. For the arabinogalactan, evidence was obtained for an interesting structure having a backbone chain of (l→3)-linked β-d-galactopyranosyl residues to which the terminal arabinose residues were attached at the C–6 position as the most prevalent side chains.     

2070-DTI,A Topoisomerase Inhibitor Produced by Streptomyces sp. Strain No. 2070

A novel inhibitor of topoisomerase II designated as 2070-DTI was isolated from the culture filtrate of Streptomyces sp. strain No. 2070. The structure was determined to be that of the known soyasaponin I on the basis of spectroscopic methods (NMR and MS). 2070-DTI strongly inhibited the decatenation activity of human placenta topoisomerase II in a noncompetitive manner, and weakly inhibited or was inert towards the relaxation activities of various topoisomerase I's and DNA-related enzymes. 2070-DTI is an inhibitor belonging to the cleavable complex-nonforming type without DNA intercalation.     

Reduction of Blood Pressure by Soybean Saponins,Renin Inhibitors from Soybean,in Spontaneously Hypertensive Rats

The effect of commercial purified soybean saponin on renin activity and blood pressure was investigated. Soybean saponin significantly inhibited human renin in vitro with IC₅₀=59.9 μg/ml. Orally administered soybean saponin at 80 mg/kg of body weight per day to spontaneously hypertensive rats for 8 weeks significantly decreased the blood pressure.     

A recently evolved BAHD acetyltransferase,responsible for bitter soyasaponin A production,is indispensable for soybean seed germination

Soyasaponins are major small molecules that accumulate in soybean (Glycine max) seeds. Among them, type-A soyasaponins, fully acetylated at the terminal sugar of their C22 sugar chain, are responsible for the bitter taste of soybean-derived foods. However, the molecular basis for the acetylation of type-A soyasaponins remains unclear. Here, we identify and characterize GmSSAcT1, encoding a BADH-type soyasaponin acetyltransferase that catalyzes three or four consecutive acetylations on type-A soyasaponins in vitro and in planta. Phylogenetic analysis and biochemical assays suggest that GmSSAcT1 likely evolved from acyltransferases present in leguminous plants involved in isoflavonoid acylation. Loss-of-function mutants of GmSSAcT1 exhibited impaired seed germination, which attribute to the excessive accumulation of null-acetylated type-A soyasaponins. We conclude that GmSSAcT1 not only functions as a detoxification gene for high accumulation of type-A soyasaponins in soybean seeds but is also a promising target for breeding new soybean varieties with lower bitter soyasaponin content.     

Renin inhibition by soyasaponin I: a potent native anti-hypertensive compound

One way to control hypertension is inactivation of the Renin- Angiotensin- Aldosterone System (RAAS). Inhibition of renin as a rate-limiting step of this system is an effective way to stop up RAAS. It has been proved that soyasaponin I, an herbal compound obtained from soybeans, has anti-hypertensive effect via renin inhibition, so it has the potential of being an anti-hypertensive drug. Herein, some theoretical approaches such as Docking Simulation, Molecular Dynamics (MD) Simulation and MMPBSA analysis have been used to study how soyasaponin I inhibits renin at the structural level. The results of docking simulation and hydrogen bond pattern show that this ligand is able to bind to the active site of renin and a region near the active site. Results of MD simulation for renin – soyasaponin I complexes confirm that soyasaponin I binds to the active site of renin and has inhibition effect on it via competing with the substrate. Besides, according to MMPBSA analysis, the binding free energy for renin – soyasaponin I complex is ?42.61 kcal/mol when it binds to the active site. Comparing to the peptide obtained from angiotensinogen, ΔG = ?74.96 kcal/mol, it may inferred that although binding of soyasaponin I to the active site of renin does not have a complete competition with the substrate, it might attenuate the formation of renin – angiotensinogen complex and have partial non-competitive effect. The results of this survey might be helpful to design partial non – competitive renin inhibitors with pharmaceutical capability.