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Fulltext Modeling of a viscoelastic damper and its application in structural control

Mehrabi MH, Suhatril M, Ibrahim Z, Ghodsi SS, Khatibi H

PLoS One, 2017;12(6):e0176480.
PMID: 28570657 DOI: 10.1371/journal.pone.0176480

Conventional seismic rehabilitation methods may not be suitable for some buildings owing to their high cost and time-consuming foundation work. In recent years, viscoelastic dampers (VEDs) have been widely used in many mid- and high-rise buildings. This study introduces a viscoelastic passive control system called rotary rubber braced damper (RRBD). The RRBD is an economical, lightweight, and easy-to-assemble device. A finite element model considering nonlinearity, large deformation, and material damage is developed to conduct a parametric study on different damper sizes under pushover cyclic loading. The fundamental characteristics of this VED system are clarified by analyzing building structures under cyclic loading. The result show excellent energy absorption and stable hysteresis loops in all specimens. Additionally, by using a sinusoidal shaking table test, the effectiveness of the RRBD to manage the response displacement and acceleration of steel frames is considered. The RRBD functioned at early stages of lateral displacement, indicating that the system is effective for all levels of vibration. Moreover, the proposed damper shows significantly better performance in terms of the column compression force resulting from the brace action compared to chevron bracing (CB).
Design and Evaluation of Curcumin-Derived Aldopentose Compounds: Unlocking their Antidiabetic Potential through Integrative In Vitro, In Vivo, and In Silico Studies on Carbohydrate-Degrading Enzymes

Routabi P, Mehrabi M, Adibi H, Mehrabi M, Khodarahmi R

J Nutr Biochem, 2025 Mar 12.
PMID: 40086674 DOI: 10.1016/j.jnutbio.2025.109897

Natural polyphenol compounds such as curcumin can inhibit carbohydrate-hydrolyzing enzymes, which may offer an alternative to expensive and potentially side-effect-inducing α-glucosidase inhibitors like acarbose. Hence, this study carried out the synthesis of curcumin aldopentose derivatives, examining their capacity to inhibit the α-glucosidase and α-amylase enzymes with the aim to alleviate hyperglycemia. Initially, the aldopentose derivatives from curcumin were synthesized and confirmed by spectroscopic methods such as MS, 13CNMR, 1HNMR, and FTIR. Afterward, we investigated the inhibitory effects of all derivatives on the α-amylase and α-glucosidase enzymes spectroscopically and determined their inhibition mechanism. We assessed the antioxidant activity and the stability of the synthetic derivatives in the simulated intestinal environment. Finally, we measured the postprandial blood glucose level after administering saturated starch in vivo. The modified compounds showed improved inhibitory effects compared to curcumin alone, with compound C3 demonstrating particularly strong enzyme inhibition. However, when compared with acarbose, a known commercial antidiabetic drug, the synthetic compounds showed lower inhibitory activity against both enzymes, resulting in fewer side effects related to undigested polysaccharides in the gut. Molecular docking studies show introducing a pentose moiety to the curcumin backbone enhanced docking affinities toward both enzymes and subsequently altered the associated IC50 and Ki values. Overall, compound C3 has the potential to be an inhibitor of carbohydrate-degrading enzymes and can effectively reduce glucose absorption in vivo. Given its antioxidant capabilities and reasonable stability, the compound in question shows promises as a potent derivative for the development of new anti-hyperglycemic drugs in future research endeavours.
Discovery of Sulfanilamide-diazo Derivatives Incorporating Benzoic Acid Moieties as Novel Inhibitors of Human Carbonic Anhydrase II Activity

Belani F, Mehrabi M, Adibi H, Mehrabi M, Khodarahmi R

Curr Protein Pept Sci, 2025;26(3):226-240.
PMID: 39648421 DOI: 10.2174/0113892037332139241008054602

BACKGROUND: Sulfonamides are widely used carbonic anhydrase inhibitors (CAIs) in clinical settings, however, their nonspecific inhibition of multiple carbonic anhydrase isoforms can lead to reduced efficacy and side effects. This study aimed to develop sulfanilamide-diazo derivatives incorporating benzoic acid moieties as novel inhibitors of hCA II activity to reduce side effects and enhance selectivity for different CA isozymes.
METHODS: We investigated the interaction between these derivatives and the hCA II isozyme via various spectroscopic and docking methods.
RESULTS: The kinetic data demonstrates that compound 1 (C1) and compound 2 (C2) share a similar inhibitory strength against hCA II, effectively inhibiting its esterase activity through a noncompetitive mechanism with Ki values at low micromolar levels. Fluorescence measurements indicated that the synthesized compounds suppressed the inherent fluorescence of hCA II via a static quenching process, with each compound showing a singular binding site within the enzyme. Thermodynamic evidences highlight the significance of van der Waals interactions and hydrogen bonding in the binding process. The results of molecular docking indicated that both C1 and C2 effectively obstruct the entrance to hCA II's active site, with no significant differences in their binding conformations.
CONCLUSION: While C1 and C2 exhibit CA inhibitory potency lower than that of sulfonamide compounds, this study offers valuable insights that could pave the way for the development of a promising scaffold for designing new carbonic anhydrase inhibitors.

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