Polysaccharides (AOPs) were extracted from Alpiniae oxyphyllae fructus using three distinct methods: hot water (AOP-HW), hydrochloric acid (AOP-AC), and NaOH/NaBH4 (AOP-AL). This study systematically investigated and compared the physicochemical properties, structural characteristics, antioxidant activities, and α-amylase inhibitory activities of the extracted polysaccharides. Among the three AOPs, AOP-AC exhibited the highest yield (13.76%) and neutral sugar content (80.57%), but had the lowest molecular weight (121.28 kDa). Conversely, AOP-HW had the lowest yield (4.54%) but the highest molecular weight (385.42 kDa). AOP-AL was predominantly composed of arabinose (28.42 mol%), galacturonic acid (17.61 mol%), and galactose (17.09 mol%), while glucose was the major sugar in both AOP-HW (52.31 mol%) and AOP-AC (94.77 mol%). Functionally, AOP-AL demonstrated superior scavenging activities against DPPH, hydroxyl, and ABTS radicals, whereas AOP-AC exhibited the strongest inhibitory effect on α-amylase. These findings indicate that the extraction solvent significantly influences the physicochemical and biological properties of AOPs, thus guiding the selection of appropriate extraction methods for specific applications. The results of this study have broad implications for industries seeking natural polysaccharides with antioxidant and enzymatic inhibitory properties.

The bioactive activity of proanthocyanidins (PAs) is closely associated with their degree of polymerization (DP), however, the effects of PAs with different DP on digestion and gut microbiota have remained unclear. To investigate this, we conducted in vitro simulated digestion and colonic fermentation studies on samples of PAs with different DP. The results showed that PAs was influenced by both protein precipitation and enzymolysis, resulting in a decrease in functional activity. PAs with a high DP were more sensitive to the gastrointestinal environment. The significant clustering trend in colonic fermentation verified the reliability of multivariate statistical techniques for screening samples with distinct functional differences. The gut microbiota analysis showed that oligomeric PAs had a stronger promoting effect on beneficial bacteria, while high polymeric PAs had a greater inhibitory effect on harmful bacteria. This study offers new insights into the biological activity and microbiological mechanisms of PAs with different DP.

UNASSIGNED: Novel α-amylase inhibitors play a crucial role in managing diabetes and obesity, contributing to improved public health by addressing these challenging and prevalent conditions. Moreover, the synthesis of anti-oxidant agents is essential due to their potential in combating oxidative stress-related diseases and promoting overall health.
UNASSIGNED: Synthesis of thoisemicarbazone derivatives of 2,4-dichlorophenyl acetic acid and to screened them for their biological activities.
UNASSIGNED: Thiosemicarbazone derivatives (4-13) were synthesized by refluxing 2,4-dichlorophenyl acetic acid with sulfuric acid in ethanol to get the ester (2), which was further refluxed with thiosemicarbazide to get compound (3). Finally, different aromatic aldehydes were refluxed with compound (3) in ethanol in catalytic amount of acetic acid to obtained the final products (4-13). Using modern spectroscopic techniques including HR-ESI-MS, 13C-, and 1H NMR, the structures of the created derivatives were confirmed.
UNASSIGNED: The synthesized derivatives showed excellent to good inhibitory activity in the range of IC50 values of 4.95 ± 0.44 to 69.71 ± 0.05 µM against α-amylase enzyme when compared to standard drug acarbose (IC50 = 21.55 ± 1.31 µM). In case of iron chelating activity, these products showed potent activity better than standard EDTA (IC50 = 66.43 ± 1.07 µM) in the range of IC50 values of 22.43 ± 2.09 to 61.21 ± 2.83 µM. However, the obtained products also show excellent to good activity in the range of IC50 values of 28.30 ± 1.17 to 64.66 ± 2.43 µM against hydroxyl radical scavenging activity when compared with standard vitamin C (IC50 = 60.51 ± 1.02 µM). DFT used to calculate different reactivity factors including ionization potential, electronegativity, electron affinity, chemical softness, and chemical hardness were calculated using frontier molecular orbital (FMO) computations. The molecular docking studies for the synthesized derivatives with α-amylase were carried out using the AutoDock Vina to understand the binding affinities with active sites of the protein.

Eleven previously undescribed lignan constituents, including five 8-O-4\' type neolignans, viburnurcosides A-E (1-5), three benzofuran type neolignans, viburnurcosides F-H (6-8), and three tetrahydrofuran type lignans, viburnurcosides I-K (9-11), were isolated from the fruits of Viburnum urceolatum. The structures of all isolates were elucidated by an extensive analysis of the NMR and HRESIMS data. The absolute configurations of these compounds were determined by quantum-chemical electronic circular dichroism calculation and comparison. The sugar units of viburnurcosides A-K were identified by acid hydrolysis and HPLC analysis of the chiral derivatives of monosaccharides. The in vitro enzyme inhibition assay exhibited that viburnurcoside J (10) had the most potent inhibitory activity against α-amylase and α-glucosidase with the IC50 values of 19.75 and 9.14 μM, respectively, which were stronger than those of the positive control acarbose (37.31 and 26.75 μM, respectively). The potential binding modes of viburnurcoside J (10) with α-amylase and α-glucosidase were also analyzed by molecular modeling.

Ten previously undescribed iridoid constituents, viburnshosins A-E (1-5) and viburnshosides A-E (6-10), together with one known analogue (11), were isolated from the branches of Viburnum chinshanense. Their structures were unambiguously elucidated by a comprehensive analysis of 1D and 2D NMR data, together with HRESIMS spectroscopic data. The absolute configurations of compounds 1-10 were assigned by means of the calculated ECD spectra. Interestingly, compounds 2 and 3 are the first iridoids with an unusual C-3-C-7 oxo bridge. Compounds 4, 5, and 10 displayed remarkable inhibitory effects against α-amylase (IC50: 38.42, 37.65, and 21.64 μM, respectively) and α-glucosidase (IC50: 12.97, 19.34, and 25.71 μM, respectively), comparable to those of the positive control acarbose (IC50: 39.75 and 23.66 μM, respectively). The interaction modes of compounds 4 and 10 with two enzymes were analyzed by molecular modeling.

The effect of gluten peptides (GPs) isolated from a gluten proteolysate on in vitro amylolysis of gelatinized wheat starch was investigated. GPs in a pepsin hydrolysate were fractionated into fractions with molecular weights (MWs) of 500-3000, 3500-7000, 10-17, and 35-48 kDa. The fractions containing peptides with MW > 10 kDa had a strong inhibitory effect on enzyme activity and amylolysis of starch, whereas GPs with MW <10 kDa had no inhibitory effect. Binding constants estimated by surface plasmon resonance showed that peptides in the fractions with MW > 10 kDa bound more strongly to α-amylase, in contrast to peptides of MW <10 kDa. Significant correlations were observed between digestion parameters and equilibrium binding affinity. We conclude that peptides with MW >10 kDa in a pepsin digest of gluten have a strong inhibitory effect on in vitro enzymatic hydrolysis of starch due to their strong binding affinity to α-amylase.

Viburnum luzonicum is widely distributed in China. Its branch extracts showed potential α-amylase and α-glucosidase inhibitory activities. In order to discover new bioactive constituents, five undescribed phenolic glycosides, viburozosides A-E (1-5), were obtained by bioassay-guided isolation coupled with HPLC-QTOF-MS/MS analysis. Their structures were elucidated by spectroscopic analyses, including 1D NMR, 2D NMR, ECD, and ORD. All compounds were tested for their α-amylase and α-glucosidase inhibitory potency. Compound 1 showed significantly competitive inhibition against α-amylase (IC50 =17.5 μM) and α-glucosidase (IC50 =13.6 μM).

α-Amylase inhibitory activity plays an important role in reducing blood glucose. Food-derived α-amylase inhibitors have attracted significant attention due to their safety. This study obtained peptides displaying α-amylase inhibitory activity from pepsin hydrolysate of quinoa protein concentrates. Gel filtration chromatography revealed that the <1 kDa component exhibited significant α-amylase inhibitory capability, while the purified component was identified via mass spectrometry identification. Six peptides with α-amylase inhibitory activity were selected, wherein the inhibitory ability of the peptide MMFPH was 66.41 % higher than the others. Molecular docking indicated that the peptide MMFPH residues restricted the α-amylase activity by binding to the active α-amylase site. The molecular interaction experiments showed that the peptides and α-amylase were in a fast-binding and slow-dissociation mode, allowing the small peptides produced via quinoa protein digestion to bind more rapidly to α-amylase, thus preventing a rise in blood glucose in vivo.

Walnut diaphragm is defined as a dry wood septum located between the walnut shell and kernel. In this work, seven phenolic compounds from walnut diaphragm were purified and characterized, and their antioxidant activities and mechanisms of hypoglycemia were investigated. Compounds 1-7 were tested for DPPH, ABTS scavenging ability, and FRAP assay to evaluate the antioxidant activity. α-Amylase inhibition assay was introduced to assess the hypoglycemic activity, and the mechanism was investigated by kinetic analysis, CD spectrum, and molecular docking. Compound 6 showed the strongest antioxidant ability, while compound 1 exhibited the strongest inhibition of α-amylase by changing the secondary structure of α-amylase in a mixed competitive inhibition mode. Molecular docking test predicted that the tetrahydropyran part in compound 1 may contribute to its hypoglycemic effect. This study furnishes a new theoretical reference for the utilization and development of walnut diaphragm into a health food with antioxidant and hypoglycemic properties. PRACTICAL APPLICATIONS: The finding of this research may serve as a basis for the subsequent development of walnut diaphragm into instant tea-based health food or added to other food carriers to achieve auxiliary antioxidant and hypoglycemic effects. This study revealed that polyphenolic components were the material basis for the antioxidant and hypoglycemic effects of walnut diaphragm, which could be identified as landmark chemical components for controlling quality standards in the development of walnut diaphragm, thus accelerating the research process of quality standards for walnut diaphragm-related products. Furthermore, the studies on the mechanism of hypoglycemic activity supply more credible data to support the development of walnut diaphragm into a safe and consumer-friendly health food. With abundant resources and clear efficacy, walnut diaphragm has great development prospect and application value.

To elucidate why the inhibitory activity of one same polyphenol against α-amylase varies in different works. Seven starchy and three artificial substrates, and a polyphenolic competitive inhibitor, tannic acid (TA) were applied to study the enzyme inhibition in different digestion systems. The results showed that the IC50 values of TA were similar for all starches at the same starch concentration, although there existed difference in starch physiochemical properties, like branching degree, amylose chain distribution, viscosity, and digestion rate. However, the IC50 values significantly decreased with the substrate concentration decreasing, regardless of substrate types. Notably, TA had a similar competitive inhibition constant (Kic) for all the starches, despite the difference in substrate concentration, indicating that the fixed constant unconditionally describes the inhibitor-enzyme binding property. In the TA/amylase/starch system, the physical adsorption of TA with starch was much weaker than the specific binding of TA with α-amylase that was driven by hydrogen bondings and π-stackings. Therefore, it was the substrate, i.e., α-1,4-glucosidic bond concentration, rather than the existing matrix of the bonds, that predominantly affected the inhibitory activity of a polyphenol, because of the competitive action between α-1,4-glucosidic bond and the polyphenol regarding binding with the enzyme.