2020
DOI: 10.1016/j.ejphar.2020.173011
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In vitro investigation of the effect of mesalazine on amyloid fibril formation of hen egg-white lysozyme and defibrillation lysozyme fibrils

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Cited by 16 publications
(11 citation statements)
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“…Moreover, other studies have shown prolongation of the lag phase of insulin aggregation [33,34]. Our previous study demonstrate that Mesalazine, in all concentrations, especially in 1:1 ratio and higher (drug to protein), had a strong inhibitory effect on lysozyme protein brillation It has been shown a direct role of aromatic ring and OH groups around the ring in the inhibitory activity of Mesalazine [15]. After con rming the inhibitory effect of Mesalazine on insulin bril formation, the effects of the compound on preformed amyloid brils was investigated.…”
Section: Discussionmentioning
confidence: 79%
See 1 more Smart Citation
“…Moreover, other studies have shown prolongation of the lag phase of insulin aggregation [33,34]. Our previous study demonstrate that Mesalazine, in all concentrations, especially in 1:1 ratio and higher (drug to protein), had a strong inhibitory effect on lysozyme protein brillation It has been shown a direct role of aromatic ring and OH groups around the ring in the inhibitory activity of Mesalazine [15]. After con rming the inhibitory effect of Mesalazine on insulin bril formation, the effects of the compound on preformed amyloid brils was investigated.…”
Section: Discussionmentioning
confidence: 79%
“…Mesalazine can be very important therapeutically in the development of new molecules that prevent the accumulation of insulin and other localized amyloidosis. In previous study, we investigated the effects of Mesalazine on the formation and elimination of amyloid brils from lysozyme proteins, in vitro [15]. According to the potent antiamyloidogenic properties of this compound on lysozyme protein, we decided to investigated the in vitro inhibitory and destabilizing effects of Mesalazine on human insulin protein brillation.…”
Section: Introductionmentioning
confidence: 99%
“…The mutations caused in HEWL protein are the main reason for genetic amyloidosis syndromes. 72 The amyloid fibrils that mount up inside due to the protein folding create natural soluble forms and misfold to generate insoluble β-sheet-rich structures. 73 We have investigated the formation of HEWL aggregates and the inhibition of aggregation in the presence of Q conjugates.…”
Section: Resultsmentioning
confidence: 99%
“…5‐aminosalicylic acid (5‐ASA) is an isomer of (4‐ASA) with a similar molecular structure, also known as mesalazine, which is a synthetic drug of non‐steroidal anti‐inflammatory drugs, and it can be used for the treatment of gastrointestinal inflammatory diseases [8]. According to research, the pharmacological and biological effects of 5‐ASA include the treatment of inflammatory bowel disease [9], as well as antioxidant [10], anti‐inflammatory [11], antibacterial [12], anticancer [13], anti‐amyloid [14], gastroprotective and anti‐fibrotic properties [15]. It can be seen that although 4‐ASA and 5‐ASA are isomers of each other, due to the different substitution positions of the amino groups, the structural differences lead to differences in the functions of the two.…”
Section: Introductionmentioning
confidence: 99%
“…T A B L E 1 The electron energies of 4-ASA and 5-ASA under the gas phase and solvent models B: COH (À15); B: OHO(14) Note: The values in parentheses represent the contribution of vibration modes, and a negative sign represents the opposite vibration phase. Abbreviations: B, bond angle bending; S, bond length stretching; T, dihedral angle torsion.…”
mentioning
confidence: 99%