In vitro and in silico analysis for elucidation of α-amylase and α-glucosidase: Synthesis, structural confirmation and drug likeness of benzothiazole derived thiazole base bis-Schiff base derivatives

Khan, Shoaib; Iqbal, Tayyiaba; Ur Rehman, Mujaddad; Hussain, Rafaqat; Khan, Yousaf; Ullah, Hayat; Ali, Mohsin; Hussain, Amjad; Alfarraj, Saleh; Ali Alharbi, Sulaiman

doi:10.1016/j.rechem.2024.101594

Results in Chemistry

2024

DOI: 10.1016/j.rechem.2024.101594

|View full text |Cite

In vitro and in silico analysis for elucidation of α-amylase and α-glucosidase: Synthesis, structural confirmation and drug likeness of benzothiazole derived thiazole base bis-Schiff base derivatives

Shoaib Khan,

Tayyiaba Iqbal,

Mujaddad Ur Rehman

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Article2

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Identification of Potential Inhibitors for Poly(ADP‐ribose) Polymerase‐10 (PARP10): Virtual Screening, Molecular Docking, and Molecular Dynamics Simulations

Lotfi,

Mohebbi,

Mohammadian Berneti

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

Poly(ADP‐ribose) polymerase‐10 (PARP10) is a critical enzyme involved in DNA damage repair. Its function in cellular repair mechanisms has been implicated in the development of chemoresistance and radioresistance in cancer cells. Consequently, PARP10 inhibition represents a promising, albeit challenging, and therapeutic target for various cancer types. This study aims to discover new PARP10 potential inhibitors via a hybrid of in silico approaches. Initially, pharmacophore‐based virtual screening was conducted on the ZINC and NCI databases. The resulting compounds were subsequently subjected to molecular docking studies to identify potential new PARP10 inhibitors. Subsequently, classical molecular dynamics (MD) simulations were conducted to evaluate and compare the dynamic behavior of the selected ligand, veliparib, and OUL35, a selective PARP10 inhibitor. Ultimately, compound ZINC20906412 was found as a potential lead compound based on its docking score and favorable interactions within the PARP10 active site. This compound may offer therapeutic potential for cancer treatment.

show abstract

Identification of Potential Inhibitors for Poly(ADP‐ribose) Polymerase‐10 (PARP10): Virtual Screening, Molecular Docking, and Molecular Dynamics Simulations

Lotfi,

Mohebbi,

Mohammadian Berneti

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

show abstract

Synthesis, Characterizations, Anti-Diabetic and Molecular Modeling Approaches of Hybrid Indole-Oxadiazole Linked Thiazolidinone Derivatives

Khan,

Iqbal,

Hussain

et al. 2024

Pharmaceuticals

View full text Add to dashboard Cite

Objective: To synthesize hybrid compounds of indole and oxadiazole in search of highly effective anti-diabetic therapeutic agent. Methods: With the goal of advancing diabetes research, our group designed and synthesized a library of 15 compounds based on indole-derived oxadiazole bearing varied substituted thiazolidinone via a multistep synthetic route. 13C-NMR, 1H-NMR and HREI-MS were applied for the characterization of all the synthesized compounds. Their biological inhibitory activity against diabetic enzymes, i.e., α-amylase and α-glucosidase was also determined. Results: Compound 7, 9 and 15 exhibited excellent inhibition against α-amylase and α-glucosidase than the standard acarbose (IC50 = 8.50 ± 0.10 µM for α-amylase and 9.30 ± 0.30 µM for α-glucosidase. To ensure the inhibitory actions of these potent analogs in molecular docking, an in silico approach was used. To determine the drug likeness of the reported analogs, an ADMET investigation was also carried out to explore the nature of the designed compounds if used as a drug. Conclusion: Fluoro-substituted analog 15 has stronger inhibition profile against both enzymes. All the potent compounds can be used as effective anti-diabetic therapeutic agents in future.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

In vitro and in silico analysis for elucidation of α-amylase and α-glucosidase: Synthesis, structural confirmation and drug likeness of benzothiazole derived thiazole base bis-Schiff base derivatives

Cited by 2 publications

References 35 publications

Identification of Potential Inhibitors for Poly(ADP‐ribose) Polymerase‐10 (PARP10): Virtual Screening, Molecular Docking, and Molecular Dynamics Simulations

Identification of Potential Inhibitors for Poly(ADP‐ribose) Polymerase‐10 (PARP10): Virtual Screening, Molecular Docking, and Molecular Dynamics Simulations

Synthesis, Characterizations, Anti-Diabetic and Molecular Modeling Approaches of Hybrid Indole-Oxadiazole Linked Thiazolidinone Derivatives

Contact Info

Product

Resources

About