Anti-amyloidogenic and fibril-destabilizing effects of two manganese–salen derivatives against hen egg-white lysozyme aggregation

Fibrillation of hen egg white lysozyme triggers reduction of copper(II)

“…In this study we have monitored the effect of Cu(II) on HEWL fibrillation at pH 7 and characterized the fibrillar species via ThT fluorescence, circular dichroism (CD) spectroscopy, fluorescence microscopy and transmission electron microscopy (TEM). Recently salen-manganese complexes have been found to exhibit potent inhibitory and disintegrating effects against HEWL fibrillation at acidic pH [34], but there is no prior report of the effect of Cu(II) on HEWL fibrillation. We report here the complete reduction of Cu(II) → Cu(I) during fibrillogenesis under aerobic conditions.…”

Effect of silybin on the fibrillation of hen egg‐white lysozyme

“…Concerning the fact that aggregation of proteins into amyloid fibrils is accompanied by a conformational change from α‐helical mode to β‐sheet, far‐UV CD was used to monitor this event. Figure A showed the far‐UV CD spectra of native HEWL, HEWL fibril (16 days old), and HEWL solution with different concentrations of silybin (incubation at 65°C for 16 days).…”

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

“…Some additives cannot only inhibit fibril formation, but they can also lead to dispersion of preformed aggregates. This is the case for the manganese–salen derivatives (Bahramikia & Yazdanparast, ; Bahramikia et al., ). The phospholipids 1,2‐dimyristoyl‐ sn ‐glycero‐3‐phophocholine and 1,2‐dihexanoyl‐ sn ‐glycerol‐3‐phosphocholine inhibit fibril formation through the binding of LYS monomers but they do not depolymerize LYS AFs (Ponikova et al., ).…”

“…Numerous researchers have investigated the inhibition of LYS amyloid formation. This has resulted in a list of compounds that either partially or completely inhibit fibril formation at acidic pH: food constituents such as short‐chain phospholipids (pH 2.0 and 55 °C) (Wang, Hung, Wen, Lin, & Chen, ), curcumin (Liu et al., ; Wang, Liu, & Lee, ) or its water‐soluble derivatives (Wang et al., ), myricetin (He et al., ), the osmolytes proline, hydroxyproline, sarcosine and trimethylamine N‐oxide (Choudhary & Kishore, ), cysteine (Takai et al., ; Wang, Liu, Wu, & Lai, ), glutathione (Wang, Chou, Liu, & Wu, ), carnosine (Wu et al., ), trehalose, magnesium chloride (Chatterjee, Kolli, & Sarkar, ), safranal, crocin (Joloudar et al., ), zinc ions (Ma, Zhang, Wang, & Zhu, ), aroma components (for example, phenyl ethyl alcohol, N,N,N,N’‐tetramethylethylenediamine, or cinnamaldehyde) (Seraj et al., ), rosmarinic acid, resveratrol (Shariatizi, Meratan, Ghasemi, & Nemat‐Gorgani, ), chemicals such as p‐benzoquinone (Lieu et al., ; Wang, Chen, & Hung, ), 4‐aminophenol and 2‐amino‐4‐chlorophenol (Vieira, Figueroa‐Villar, Meirelles, Ferreira, & De Felice, ), tris(2‐carboxyethyl)phosphine (Wang, Liu, & Lu, ), SDS concentrations of at least 0.25 mM (Hung et al., ), nonionic detergents like triton X‐100 and n‐dodecyl‐β‐D‐maltoside (Siposova, Kozar, & Musatov, ), the ionic liquid tetramethyl guanidinium acetate (Kalhor, Kamizi, Akbari, & Heydari, ), clotrimazole (Sarkar, Kumar, & Dubey, ), sodium tetrathionate (Sarkar, Kumar, & Dubey, ), β‐mercaptoethanol (Sarkar et al., ), glycol‐acridines (Vuong et al., ), 2‐acetyl amin‐3‐[4‐(2‐amintgo‐5‐sulfo‐phenyl]‐propionic acid (Maity et al., ), indole, indole 3‐acetic acid, indole 3‐carbinol, indole 3‐propionic acid and tryptophol (Morshedi, Rezaei‐Ghaleh, Ebrahim‐Habibi, Ahmadian, & Nemat‐Gorgani, ), and other components such as melatonin (Wang, Chen, et al., ), glutathione‐covered gold nanoparticles (Antosova et al., ), manganese–salen derivatives (Bahramikia & Yazdanparast, ; Bahramikia, Yazdanparast, & Gheysarzadeh, ), the crowding agents Ficoll 70 and dextran 70 (Ma et al., ), bovine serum albumin and its combination with Ficoll 70 (Zhou, Zhou, Hu, Chen, & Liang, ), and type I collagen (Dubey & Mar, ).…”