Exploring the possibility of familiar dietary sources as additional diabetes treatments is crucial, especially considering the financial difficulties related to diabetes mellitus. Using both in vitro and in silico techniques, this work aims to assess the antidiabetic benefits of extract from Solanum lasiocarpum Dunal. The evaluations encompass the ability to scavenge DPPH radicals, inhibition of α-amylase, α-glucosidase, inhibition of DPP-4, cytotoxicity, and glucose absorption kinetics. With an IC50 value of 0.69 ± 0.14 mg/ml, S. lasiocarpum showed encouraging DPPH inhibition. IC50 values of 2.123 ± 0.14 mg/ml inhibited the enzymes α-amylase, α-glucosidase, and DPP-4. Furthermore, a notable increase (P < 0.05) in glucose uptake by L6 myoblasts was observed with the administration of various combinations. In silico analysis, including XP docking and MM-GBSA, revealed that 10 and 21 compounds within the combination exhibited substantial interactions and stable binding capabilities with α-amylase and DPP-4 proteins, indicating their potential as enzyme inhibitors. Therefore, it can be inferred that S. lasiocarpum represents a promising therapeutic approach for diabetes management.
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Chem Biodivers
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Indian Institute of Technology Guwahati, Biosciences and Bioengineering, BSBE, Guwhati, INDIA.
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National Key Laboratory of Crop Genetic Improvement, Huazhong Agricultural University, Wuhan, 430070, China.
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BMC Chem
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Department of Physics, Faculty of Engineering, Hacettepe University, Beytepe-Ankara, Çankaya, 06800, Turkey.
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Department of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany. Electronic address:
Upregulation of the actin-severing protein Cofilin-1 is implicated in enhancing malignancy of various cancer types by promoting actin turnover and increasing cellular motility. Despite the importance of targeting Cofilin-1, currently there is a lack of inhibitors specifically targeting its actin-severing activity. To address this issue, we generated synthetic anti-Cofilin-1 nanobodies (Sybodies) that interfere with human Cofilin-1 binding to filamentous actin.
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