65372-43-2Relevant academic research and scientific papers
One-step partial synthesis of (±)-asperteretone B and related hPTP1B1–400 inhibitors from butyrolactone I
Coporo-Blancas, Diego,Morales-Jiménez, Jesús,Rivera-Chávez, José
, (2020)
Protein tyrosine phosphatase 1B (PTP1B) is a validated target for developing antiobesity, antidiabetic and anticancer drugs. Over the past years, several inhibitors of PTP1B have been discovered; however, none has been approved by the drug regulatory agencies. Interestingly, the research programs focused on discovering PTP1B inhibitors typically use truncated structures of the protein (PTP1B1-300, 1–300 amino acids), leading to the loss of valuable information about the inhibition and selectivity of ligands and repeatedly misleading the optimization of putative drug leads. Up to date, only six inhibitors of the full-length protein (hPTP1B1-400), with affinity constants ranging from 1.3 × 104 to 3.3 × 106 M?1, have been reported. Towards the discovery of new ligands of the full-length human PTP1B (hPTP1B1-400) from natural sources, herein we describe the isolation of a γ-lactone (1, butyrolactone I) from the fungus Aspergillus terreus, as well as the semisynthesis, inhibitory properties (in vitro and in silico), and the structure-activity relationship of a set of butyrolactone derivatives (1 and 2, and 6–12) as hPTP1B1-400 inhibitors, as well as the affinity constant (ka = 2.2 × 105 M?1) of the 1-hPTP1B1–400 complex, which was determined by fluorescence quenching experiments, after the inner filter effect correction.
Effect on α-glucosidase inhibition and antioxidant activities of butyrolactone derivatives from Aspergillus terreus MC751
Dewi, Rizna Triana,Tachibana, Sanro,Darmawan, Ahmad
, p. 454 - 460 (2014/03/21)
Butyrolactone I and II from Aspergillus terreus MC751 as well as three synthetic butyrolactone I derivatives were assessed for α-glucosidase inhibitory and antioxidant activities. Butyrolactone I (1), which has a prenyl side chain and an alpha hydroxy-lactone group, was the most potent α-glucosidase inhibitor and also had antioxidant activities with IC 50 values of 52.17 ± 5.68 and 51.39 ± 3.68 μM, respectively. In contrast, butyrolactone II (2) lacking a prenyl side chain was the most potent antioxidant with an IC50 of 17.64 ± 6.41 μM, but was less active against α-glucosidase. Acetylation of all hydroxyl groups of butyrolactone I significantly decreased both the α-glucosidase inhibitory and antioxidant activity. The prenyl and alpha hydroxy-lactone groups seem to have a synergic effect on the inhibitory activity but not antioxidant activity. This is the first structure-activity relationship report on the α-glucosidase inhibition and antioxidant activity by butyrolactone derivatives.
Aspernolides A and B, butenolides from a marine-derived fungus Aspergillus terreus
Parvatkar, Rajesh R.,D'Souza, Celina,Tripathi, Ashootosh,Naik, Chandrakant G.
experimental part, p. 128 - 132 (2009/07/25)
Two aromatic butenolides, aspernolides A and B along with the known metabolites, butyrolactone I, terrein and physcion were isolated from the fermentation broth of a soft coral derived fungus Aspergillus terreus. The structures of these metabolites were a
