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Original Article
ARTICLE IN PRESS
doi:
10.25259/AJC_219_2026

Oxindole-pyrrole-piperazine hybrids as novel α-glucosidase inhibitors: Design, synthesis and evaluation

, , , ,
aSchool of Engineering and Science, Faculty of Engineering, Computing and Science, Swinburne University of Technology Sarawak Campus, Sarawak, Malaysia
bFaculty of Applied Sciences, MARA University of Technology (UiTM), Sarawak Branch, Sarawak, Malaysia

*Corresponding author: E-mail address: bguo@swinburne.edu.my (B. Guo)

Received: , Accepted: ,
© 2026 Arabian Journal of Chemistry - Published by Scientific Scholar
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This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial-Share Alike 4.0 License, which allows others to remix, transform, and build upon the work non-commercially, as long as the author is credited and the new creations are licensed under the identical terms.

Abstract

α-Glucosidase acts as one therapeutic target for diabetes. For finding novel α-glucosidase inhibitors, oxindole-pyrrole-piperazine hybrids (OPP-1∼24) were synthesized. Inhibition evaluation revealed that all hybrids (OPP-1∼X24) demonstrated potent α-glucosidase inhibitory activity with IC50 values of 6.34 ∼ 27.95 μM, obviously better than that of acarbose. Among them, OPP-11, as the strongest inhibitor (IC50 = 6.34 μM), acted as a mixed-type inhibitor. Fluorescence quenching experiments indicated interaction of OPP-11 with α-glucosidase following a static quenching mechanism. Circular dichroism and 3D fluorescence results revealed OPP-11 binding induced α-glucosidase conformation changes. Molecular docking simulations further elucidated the detailed binding mode of OPP-11 on α-glucosidase. Collectively, the oxindole-pyrrole-piperazine scaffold represents a promising template to find α-glucosidase inhibitors.

Keywords

α-Glucosidase
Inhibition mechanism
Oxindole
Piperazine
Pyrrole

1. Introduction

Diabetes, a chronic metabolic disorder, mainly results from insufficient insulin secretion [1]. Diabetes has the main clinical symptom of persistent hyperglycemia, and long-term illness would induce cardiovascular and cerebrovascular diseases [2,3]. Now, α-glucosidase inhibitors have been used to reduce postprandial hyperglycemia, and play pivotal roles in digestion and are essential for blood glucose regulation [4]. It can degrade and absorb carbohydrates, consequently leading to an elevation in postprandial blood glucose levels [5]. At present, several α-glucosidase inhibitors are widely used in clinical, however, their prolonged use may lead to gastrointestinal adverse effects [6]. Consequently, it’s necessary to develop novel α-glucosidase inhibitors.

Natural products serve as indispensable resources in the field of drug development [7-9]. Many clinical drugs are derived from natural products and derivatives [10-12]. Oxindole, one indole compound, exists in various natural products. Oxindole and its derivatives exhibit α-glucosidase inhibitory activity (Figures 1a and b) [13,14]. Thence, oxindole would be one potential scaffold for developing novel α-glucosidase inhibitors. Pyrrole is a representative heterocyclic compound; its derivatives exhibit many biological activities [15]. Meanwhile, pyrrole is employed to develop α-glucosidase inhibitors (Figures 1c), as the presence of the pyrrole ring may alter the chemical and spatial structure of the inhibitors, enabling them to better bind to the α-glucosidase active site [16]. Piperazine, another important heterocyclic compound, also plays a pivotal role in pharmaceutical development. It can enhance the solubility and stability of drugs while optimizing their pharmacokinetic properties [17]. Moreover, recent studies have reported the utilization of piperazine in the design of α-glucosidase inhibitors (Figures 1d) [18].

(a) Previous reported α-glucosidase inhibitors [13, 14,16, 18] and (b) Design strategy.
Figure 1. (a) Previous reported α-glucosidase inhibitors [13, 14,16, 18] and (b) Design strategy.

The strategy of molecular hybridization has emerged as a powerful approach in drug discovery, which involves the combination of two or more bioactive pharmacophores into a single new chemical entity [19-21]. This method can potentially lead to improved affinity, modified selectivity, or reduced toxicity compared to the parent molecules [22,23]. In this study, we applied a hybridization strategy to develop a series of novel α-glucosidase inhibitors (oxindole-pyrrole-piperazine hybrids, OPP-1∼24) (Figure 1b), followed by synthesis and biological activity evaluation.

2. Materials and Methods

2.1. Synthesis of oxindole derivatives (OPP-1∼24)

A sodium hydroxide solution was first prepared by dissolving NaOH (2.012 g, 50.32 mmol) in ethanol (175 mL). To a 500 mL round-bottom flask charged with 2-indolone (S1, 958 mg, 7.19 mmol) and 5-formyl-1H-pyrrole-2-carboxylic acid (S2, 1000 mg, 7.19 mmol), the freshly prepared NaOH/EtOH solution was added dropwise under ice-bath cooling. After the reaction was completed, the solution was adjusted pH to 7 using 1 N HCl. The solid (crude product S3) was collected by filtration to afford. In a 35 mL sealed tube, intermediate S3 (70 mg, 0.2755 mmol), the corresponding substituted phenylpiperazine (0.3306 mmol), and 1-(3-Dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride (EDCI) (80 mg, 0.4132 mmol) were added in pyridine (3 mL). Upon completion, excess hydrochloric acid was added. The resulting solid was recrystallized from ethanol to afford target compounds OPP-1∼24. All compounds were characterized by 1H NMR, 13C NMR, and HRMS, and the data were summarized in the Supporting Information.

Supporting Information

2.2. α-Glucosidase inhibition and kinetics assay

α-Glucosidase inhibition of OPP-1∼24 was evaluated using p-nitrophenyl α-D-glucopyranoside (p-NPG) as the substrate [24]. α-Glucosidase (from Saccharomyces cerevisiae, 0.05 U/mL, final concentration) and the test compounds were dissolved in phosphate buffer saline (PBS) buffer (0.1 M, pH 6.8) and pre-incubated at 37°C for 10 min. The final concentration of DMSO in the reaction mixture was maintained at 5.0% (v/v). After adding p-NPG (1 mM, final concentration), the absorbance was measured at 405 nm using a microplate reader. For the inhibition mechanism and kinetics, the inhibitory activity of OPP-11 was determined at different enzyme concentrations (0.0375-0.075 U/mL, final concentrations) to obtain the enzyme activity curves. For the inhibition type, the activity of OPP-11 was measured with varying substrate concentrations (1.0–4.0 mM, final concentrations) to yield lineweaver-burk plots [25]. All assays were performed in quadruplicate (n = 4).

2.3. Fluorescence quenching

The quenching assay of α-glucosidase by OPP-11 was carried out upon excitation at 280 nm [26,27]. OPP-11 was added sequentially to the α-glucosidase solution (0.1 mg/mL) in a quartz cuvette. The fluorescence spectra were recorded in the range of 300–450 nm using a fluorescence spectrophotometer. The final concentrations of OPP-11 ranged from 0 to 6.5 μM.

2.4. 3D fluorescence spectra

The 3D fluorescence spectra of α-glucosidase and the α-glucosidase-OPP-11 complex were recorded with excitation and emission wavelengths ranging from 200 to 500 nm [28,29]. The final concentration of α-glucosidase was maintained at 0.1 mg/mL, while the final concentration of OPP-11 was 5.0 μM. The mixture was equilibrated in PBS buffer (0.1 M, pH 6.8) for 10 min at room temperature before measurement to ensure stable complex formation.

2.5. CD spectra

CD spectra of α-glucosidase-OPP-11 were determined according to previous reports [30]. The enzyme concentration was 70 μM in PBS buffer (0.1 M, pH 6.8). The final concentrations of OPP-11 were set at 0, 70, 140, and 210 μM, respectively. The spectra were recorded from 200 to 250 nm. The secondary structure contents were calculated using circular dichroism spectra deconvolution software (CDNN).

2.6. Molecular docking

The molecular docking simulation was performed using AutoDock Vina (version 1.2.3) [31-33]. Due to the absence of a crystal structure for α-glucosidase from saccharomyces cerevisiae, the crystal structure of isomaltase from the same source (PDB ID: 3A4A) was utilized as the docking receptor. Prior to docking, water molecules were removed, and polar hydrogens were added to the protein using AutoDockTools. The active site was defined by a grid box of 15.44 Å × 15.44 Å × 15.44 Å, centered at coordinates (x: 16.549, y: -7.433, z: 16.455). The exhaustiveness was set to 8. The best-scoring pose with the lowest binding affinity was selected for further interaction analysis using PyMOL [34,35].

3. Results and Discussion

3.1. Chemistry

OPP-1∼24 were synthesized as depicted in Scheme 1. The intermediate S3 was obtained via the condensation reaction between 2-oxindole (S1) and 5-formyl-1H-pyrrole-2-carboxylic acid (S2) under alkaline conditions. Subsequently, the intermediate S3 underwent the condensation reaction with substituted phenylpiperazine, yielding the target product OPP-1∼24.

(a) NaOH, Ethanol (EtOH), r.t.; (b) EDCI, Pyridine, substituted phenylpiperazine, r.t.
Scheme 1. (a) NaOH, Ethanol (EtOH), r.t.; (b) EDCI, Pyridine, substituted phenylpiperazine, r.t.

3.2. α-Glucosidase activity

OPP-1∼24 were evaluated for α-glucosidase inhibitory activity. The results suggested that hybrids (OPP-1∼24) demonstrated potent inhibitory activity, and IC50 values ranged from 6.34 ± 0.33 to 27.95 ± 1.28 μM (Table 1). All hybrids presented stronger activity than acarbose (IC50 = 596.84 ± 49.90 μM). Especially, the most promising compound OPP-11 exhibited an activity 94 times higher than acarbose. Thence, hybridization of oxindole with pyrrole and piperazine to form a novel compound represented a promising strategy for developing effective α-glucosidase inhibitors.

Table 1. Inhibition of OPP-1∼24 on α-glucosidase.
Compounds R IC50 (μM) Compounds R IC50 (μM)
OPP-1 H 27.95 ± 1.28 OPP-13 3-OCH3 25.64 ± 1.28
OPP-2 2-F 24.96 ± 0.55 OPP-14 4-OCH3 10.51 ± 1.12
OPP-3 4-F 20.57 ± 0.65 OPP-15 2-CN 40.80 ± 1.22
OPP-4 2-Cl 14.42 ± 0.65 OPP-16 3-CN 9.15 ± 0.30
OPP-5 3-Cl 13.76 ± 2.79 OPP-17 4-CN 10.45 ± 1.25
OPP-6 4-Cl 9.87 ± 0.29 OPP-18 2-NO2 25.78 ± 0.55
OPP-7 3-Br 6.67 ± 0.89 OPP-19 3-NO2 9.73 ± 0.25
OPP-8 4-Br 13.81 ± 0.80 OPP-20 4-NO2 8.74 ± 1.21
OPP-9 2-CH3 9.95 ± 2.59 OPP-21 2-OH 27.91 ± 2.38
OPP-10 3-CH3 7.41 ± 0.04 OPP-22 3-OH 20.32 ± 1.93
OPP-11 4-CH3 6.34 ± 0.33 OPP-23 4-OH 23.83 ± 0.51
OPP-12 2-OCH3 27.74 ± 0.55 OPP-24 4-CF3 10.63 ± 2.38
Acarbose 596.84 ± 49.90

An analysis of the structure-activity relationship (SAR) revealed that the biological potency was significantly modulated by the electronic properties and hydrophobicity of the substituents on the terminal benzene ring. Regarding electronic effects, derivatives bearing electron-withdrawing groups such as -NO2 (OPP-20, IC50 = 8.74 μM), -CN (OPP-16, 9.15 μM), and -Cl (OPP-6, 9.87 μM) generally exhibited superior activity compared to the unsubstituted OPP-1 (27.95 μM). This suggests that an electron-deficient phenyl ring may strengthen the π-π stacking interactions with aromatic amino acid residues in the active site of α-glucosidase. Interestingly, the exceptional activity of OPP-11 (4-CH3) highlights the importance of hydrophobic interactions. Although the methyl group is an electron-donating group, its balanced lipophilicity (ClogP) and size likely allow for optimal complementarity with the hydrophobic pockets of the enzyme. Furthermore, a general positional trend was observed where para- and meta-substitutions were significantly more effective than ortho-substitutions. This can be attributed to the steric hindrance at the ortho-position, which may restrict the molecule from adopting a favorable conformation to enter the catalytic site.

3.3. Kinetic studies

The inhibition properties of OPP-11 on the enzyme were investigated. The enzymatic reaction curves with different OPP-11 concentrations intersected at the origin (Figure 2a), indicating that OPP-11 could reversibly inhibit enzyme activity. The inhibition type of OPP-11 on the enzyme was determined by lineweaver-burk plots. Obtained linear lines intersected in the third quadrant, with both slope and Y-intercept exhibiting a positive correlation with OPP-11 concentrations (Figure 2b). The results indicated that OPP-11 exerted as a mixed-type inhibitor, suggesting that OPP-11 could bind to α-glucosidase and the α-glucosidase-substrate complex, inhibiting the activity.

(a) Enzymatic reaction curves; (b) Lineweaver-Burk plots.
Figure 2. (a) Enzymatic reaction curves; (b) Lineweaver-Burk plots.

3.4. Fluorescence quenching

The fluorescence quenching performance of OPP-11 on α-glucosidase was investigated to evaluate binding features. α-Glucosidase exhibited fluorescence at 345 nm, whereas OPP-11 had no obvious fluorescence (Figures 3a-c). Following the treatment of OPP-11, α-glucosidase fluorescence intensity progressively diminished, suggesting that OPP-11 was capable to quench α-glucosidase fluorescence.

Furthermore, the Stern-Volmer plot (Figure 3d) demonstrated a linear relationship, indicating the presence of a single quenching mechanism. The quenching constant was obtained through calculation (Table 2). The Kq values were markedly higher than 2×1010 L mol-1s-1, and Ksv values reduced with temperature. Consequently, OPP-11 could quench α-glucosidase in a static process. Moreover, Ka values reached a level of 103, which indicated moderate strength binding of OPP-11 with α-glucosidase.

(a-c) Quenching of OPP-11 on α-glucosidase; (d) Stern-Volmer plots of OPP-11.
Figure 3. (a-c) Quenching of OPP-11 on α-glucosidase; (d) Stern-Volmer plots of OPP-11.
Table 2. Quenching constants of compound OPP-11 on α-glucosidase.
T (K) Kq (× 1012 Lmol-1) Ksv (× 104Lmol-1) Ka (× 103Lmol-1)
310 6.83 6.83 2.71
304 4.53 4.53 1.09
298 3.88 3.88 10.498

3.5. 3D fluorescence spectra

The effects of OPP-11 on α-glucosidase conformation were assessed. As shown in Figure 4(a), α-Glucosidase exhibited the characteristic peaks. Among them, peak 1 was attributed to the emission from tyrosine and tryptophan residues, while peak 2 corresponded to the peptide backbone’s structural characteristics. Following OPP-11 treatment (Figure 4b), the peaks intensity was observed to decrease, suggesting that OPP-11 could interact with fluorescent residues of α-glucosidase, possibly altering the microenvironment and conformation of the protein.

(a-b) 3D fluorescence of α-glucosidase without/with OPP-11.
Figure 4. (a-b) 3D fluorescence of α-glucosidase without/with OPP-11.

3.6. CD spectra

The effects of OPP-11 on α-glucosidase secondary structure were assessed. It was observed from CD spectra that α-glucosidase exhibited the negative band around 210∼220 nm (Figure 5). The addition of OPP-11 would cause the changes in α-glucosidase CD spectra, indicating secondary structure changes of α-glucosidase. Analyzing the changes, OPP-11 could increase α-helix, β-turn, and random coil contents, and reduce β-sheet content (Table 3). The secondary content changes caused by OPP-11 would be the main reasons for enzyme activity reduction.

CD spectra of α-glucosidase with OPP-11.
Figure 5. CD spectra of α-glucosidase with OPP-11.
Table 3. α-Glucosidase secondary structure (%) upon OPP-11.
[Enzyme]: [OPP-11] α-Helix β-Sheet β-Turn Random coil
1:0 17.84 31.41 19.56 36.74
1:1 18.69 22.31 20.34 43.87
1:2 18.70 22.20 20.39 44.26
1:3 18.83 22.09 21.29 44.44

3.7. Molecular docking

To better understand binding interactions between OPP-11 and α-glucosidase, AutoDock Vina software was used to conduct the docking of OPP-11 and α-glucosidase. As shown in Figure 6, the most active compound, OPP-11, exhibited a strong binding affinity to α-glucosidase with a binding energy of -10.4 kcal/mol. The docking analysis revealed that the indole NH of OPP-11 established a strong hydrogen bond with the side chain of GLU-277 (distance: 2.1 Å), while the carbonyl oxygen anchored the molecule via a hydrogen bond with GLN-279 (2.7 Å). The scaffold was further stabilized by hydrophobic interactions within the catalytic gorge. Specifically, the phenyl ring and pyrrole moiety were involved in hydrophobic contacts with aromatic residues, including ASP-69, TYR-72, PHE-159, PHE-178, ASP-215, PHE-303 and THR-310, which accounts for its exceptional inhibitory potency.

(a-c) Binding of OPP-11 with α-glucosidase. (d) Interactions of OPP-11 with α-glucosidase.
Figure 6. (a-c) Binding of OPP-11 with α-glucosidase. (d) Interactions of OPP-11 with α-glucosidase.

4. Conclusions

Twenty-four novel oxindole-pyrrole-piperazine hybrids (OPP-1∼24) were designed based on scaffold hopping and hybridization strategies. α-Glucosidase inhibitory activity screening found that all synthesized hybrids (OPP-1∼24) exhibited potent inhibitory effects, significantly stronger than acarbose. OPP-11 emerged as the most active derivative, functioning as a mixed-type inhibitor. Mechanistic investigations revealed that OPP-11 quenched the intrinsic fluorescence of α-glucosidase through a static quenching process. Conformational analyses using CD and 3D fluorescence spectra demonstrated that OPP-11 induced secondary structural alterations in the enzyme. Molecular docking further elucidated the key interactions between OPP-11 and the enzyme active site. However, we have provided a novel indole-pyrrole-piperazine hybrids as α-glucosidase inhibitors and studied their activity and inhibition mechanism. However, the effectiveness and safety of hybrids have not been validated in cell or animal models, which could be the future research focus.

CRediT authorship contribution statement

Bao Guo: Concept and design of the study, acquisition of data, and final approval of the version to be published. Irine Runnie Ginjom, Zhen Liu, Heng Yen Khong, and Lee Tung Tan: Analysis and interpretation of data.

Declaration of competing interest

There are no conflicts of interest.

Data availability

The datasets presented in the current study are available from the corresponding author upon reasonable request.

Declaration of generative AI and AI-assisted technologies in the writing process

The authors confirm that there was no use of artificial intelligence (AI)-assisted technology for assisting in the writing or editing of the manuscript, and no images were manipulated using AI.

Supplementary data

Supplementary material to this article can be found online at https://dx.doi.org/10.25259/AJC_219_2026.

References

  1. , , , , , , , , , , . Synthesis and anti-α-glucosidase activity evaluation of betulinic acid derivatives. Arabian Journal of Chemistry. 2023;16:104659. https://doi.org/10.1016/j.arabjc.2023.104659
    [Google Scholar]
  2. , , , , , , , . Synthesis and biological evaluation of coumarin derivatives containing oxime ester as α-glucosidase inhibitors. Arabian Journal of Chemistry. 2022;15:104072. https://doi.org/10.1016/j.arabjc.2022.104072
    [Google Scholar]
  3. , , , , , , , , . Identification of 1,3,4-thiadiazolyl-containing thiazolidine-2,4-dione derivatives as novel PTP1B inhibitors with antidiabetic activity. Journal of Medicinal Chemistry. 2024;67:8406-8419. https://doi.org/10.1021/acs.jmedchem.4c00676
    [Google Scholar]
  4. , , , . Novel thiosemicarbazide-based β-carboline derivatives as α-glucosidase inhibitors: Synthesis and biological evaluation. European Journal of Medicinal Chemistry. 2024;275:116595. https://doi.org/10.1016/j.ejmech.2024.116595
    [Google Scholar]
  5. , , , , , , . Synthesis, anti-α-glucosidase activity, inhibition interaction, and anti-diabetic activity of novel cryptolepine derivatives. Journal of Molecular Structure. 2024;1310:138311. https://doi.org/10.1016/j.molstruc.2024.138311
    [Google Scholar]
  6. , , , . Novel sulfonyl hydrazide based β-carboline derivatives as potential α-glucosidase inhibitors: Design, synthesis, and biological evaluation. Molecular Diversity. 2025;29:1669-1681. https://doi.org/10.1007/s11030-024-10943-4
    [Google Scholar]
  7. , , , , , , , . Structural characteristics and anticancer/antioxidant activities of a novel polysaccharide from Trichoderma kanganensis. Carbohydrate Polymers. 2019;205:63-71. https://doi.org/10.1016/j.carbpol.2018.09.068
    [Google Scholar]
  8. , , , , , , , , , , , , , , . Unique structure and biological properties of fucosylated glycosaminoglycan and its oligosaccharides from sea cucumber Holothuria floridana. Carbohydrate Polymers. 2025;355:123351. https://doi.org/10.1016/j.carbpol.2025.123351
    [Google Scholar]
  9. , , , , , , , , , , . Structural elucidation of an active polysaccharide from Radix Puerariae lobatae and its protection against acute alcoholic liver disease. Carbohydrate Polymers. 2024;325:121565. https://doi.org/10.1016/j.carbpol.2023.121565
    [Google Scholar]
  10. , , , , , , , . Polysaccharide produced by Bacillus subtilis using burdock oligofructose as a carbon source. Carbohydrate Polymers. 2019;206:811-819. https://doi.org/10.1016/j.carbpol.2018.11.062
    [Google Scholar]
  11. , , , , , . Rhizopus nigricans polysaccharide activated macrophages and suppressed tumor growth in CT26 tumor-bearing mice. Carbohydrate Polymers. 2018;198:302-312. https://doi.org/10.1016/j.carbpol.2018.06.076
    [Google Scholar]
  12. , , , , . A combination of selenium and polysaccharides: Promising therapeutic potential. Carbohydrate Polymers. 2019;206:163-173. https://doi.org/10.1016/j.carbpol.2018.10.088
    [Google Scholar]
  13. , , , , , , , , . Towards multi-target antidiabetic agents: In vitro and in vivo evaluation of 3,5-disubstituted indolin-2-one derivatives as novel α-glucosidase inhibitors. Bioorganic & Medicinal Chemistry Letters. 2022;55:128449. https://doi.org/10.1016/j.bmcl.2021.128449
    [Google Scholar]
  14. , , , , . Design, synthesis, and in vitro study of densely functionalized oxindoles as potent α-glucosidase inhibitors. Bioorganic & Medicinal Chemistry. 2018;26:4996-5005. https://doi.org/10.1016/j.bmc.2018.08.022
    [Google Scholar]
  15. , , , , , , , . Thieno[3,2-b]pyrrole as a privileged scaffold in medicinal chemistry: An exploration of synthetic strategies and anticancer attributes. Journal of Molecular Structure. 2025;1321:139654. https://doi.org/10.1016/j.molstruc.2024.139654
    [Google Scholar]
  16. , , , . Design, synthesis, and molecular docking study of novel pyrrole-based α-amylase and α-glucosidase inhibitors. Medicinal Chemistry Research. 2017;26:2675-2691. https://doi.org/10.1007/s00044-017-1965-z
    [Google Scholar]
  17. , , , , , . An appraisal of anti-mycobacterial activity with structure-activity relationship of piperazine and its analogues: A review. European Journal of Medicinal Chemistry. 2021;210:112967. https://doi.org/10.1016/j.ejmech.2020.112967
    [Google Scholar]
  18. , , , , , . Novel coumarin-thiazolidine-2,4 dione hybrids as potential α-glucosidase inhibitors: Synthesis and bioactivity evaluation. Journal of Molecular Structure. 2025;1322:140481. https://doi.org/10.1016/j.molstruc.2024.140481
    [Google Scholar]
  19. , , , , , , , , , , , , , , , , , , , , . Discovery of novel PROTAC SIRT6 degraders with potent efficacy against hepatocellular carcinoma. Journal of Medicinal Chemistry. 2024;67:17319-17349. https://doi.org/10.1021/acs.jmedchem.4c01223
    [Google Scholar]
  20. , , , , , , , , , , , , , . Discovery of a photoactivatable dimerized STING agonist based on the benzo[b]selenophene scaffold. Chemical Science. 2023;14:4174-4182. https://doi.org/10.1039/d2sc06860e
    [Google Scholar]
  21. , , , , , , , , , . Discovery of selective CDK9 degraders with enhancing antiproliferative activity through PROTAC conversion. European Journal of Medicinal Chemistry. 2021;211:113091. https://doi.org/10.1016/j.ejmech.2020.113091
    [Google Scholar]
  22. , , , , , , , . The SAR and action mechanisms of autophagy inhibitors that eliminate drug resistance. European Journal of Medicinal Chemistry. 2022;244:114846. https://doi.org/10.1016/j.ejmech.2022.114846
    [Google Scholar]
  23. , , , , , , , , , , , , , , , , . Structure-enabled discovery of novel macrocyclic inhibitors targeting glutaminase 1 allosteric binding site. Journal of Medicinal Chemistry. 2021;64:4588-4611. https://doi.org/10.1021/acs.jmedchem.0c02044
    [Google Scholar]
  24. , , , , , , . Thiazolidine-2,4-dione derivatives as potential α-glucosidase inhibitors: Synthesis, inhibitory activity, binding interaction, and hypoglycemic activity. Bioorganic Chemistry. 2024;144:107177. https://doi.org/10.1016/j.bioorg.2024.107177
    [Google Scholar]
  25. , , , , . Rosa × damascena Herrm. essential oil: Anti-tyrosinase activity and phytochemical composition. Frontiers in Pharmacology. 2024;15:1451452. https://doi.org/10.3389/fphar.2024.1451452
    [Google Scholar]
  26. , , , . Investigation on the inhibition mechanism and binding behavior of cryptolepine to α-glucosidase and its hypoglycemic activity by multi-spectroscopic method. Journal of Luminescence. 2024;269:120437. https://doi.org/10.1016/j.jlumin.2024.120437
    [Google Scholar]
  27. , , , , , , . Synthesis and biological evaluation of indole derivatives containing thiazolidine-2,4-dione as α-glucosidase inhibitors with antidiabetic activity. European Journal of Medicinal Chemistry. 2024;264:115957. https://doi.org/10.1016/j.ejmech.2023.115957
    [Google Scholar]
  28. Zhou, H., Wen, Y., Wang, S.H., Liu, Y., Li, B., Xu, X., 2025. Thiadiazole based β-carboline derivatives as potential α-glucosidase inhibitors: Design, synthesis, and bioactivity evaluation. Molecular Diversity, 2025 Oct 5 (last accessed 27 Feb 2026). https://doi.org/10.1007/s11030-025-11369-2
  29. , , . Inhibition mechanisms of daidzein and genistein against α-amylase and α-glucosidase. International Journal of Biological Macromolecules. 2025;333:148794. https://doi.org/10.1016/j.ijbiomac.2025.148794
    [Google Scholar]
  30. Wen, Y., Yu, Q., Yang, F., Li, J., Lang, M., Yan, J.L., Xu, X., 2026. Synthesis and biological evaluation of novel Kojic acid-cinnamic acid hybrids as tyrosinase inhibitors. Molecular Diversity, 2026 Mar 1 (last accessed 27 Feb 2026). https://doi.org/10.1007/s11030-026-11487-5
  31. , , , , , , , , , , , , . Discovery of novel thiophene[2,3-d]pyrimidine-thiazole derivative as promising MNK inhibitor to treat breast cancer. Journal of Molecular Structure. 2025;1321:140125. https://doi.org/10.1016/j.molstruc.2024.140125
    [Google Scholar]
  32. , , , , , , , , , . Near-infrared organic photosensitizers with aggregation-induced emission and switchable fluorescence for fungal infection therapy. Science China Chemistry. 2025;68:1426-1433. https://doi.org/10.1007/s11426-024-2325-2
    [Google Scholar]
  33. , , , , , , . Drug development and potential targets for Cushing’s syndrome. European Journal of Medicinal Chemistry. 2024;270:116333. https://doi.org/ 10.1016/j.ejmech.2024.116333
    [Google Scholar]
  34. , , , , , , , , , . A highly sensitive Lock-Cas12a biosensor for detection and imaging of miRNA-21 in breast cancer cells. Talanta. 2024;273:125938. https://doi.org/10.1016/j.talanta.2024.125938
    [Google Scholar]
  35. , , , , , , , , , , , , , , , , , , , , , , , , , . Proteomic profiling of urinary large extracellular vesicles for the diagnosis of prostate cancer. Analytical Chemistry. 2025;97:17368-17379. https://doi.org/10.1021/acs.analchem.5c01320
    [Google Scholar]

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