Interaction of ectoine and hydroxyectoine with protein: fluorescence study

Rasteniene, Auguste; Gruškienė, Rūta; Sereikaitė, Jolanta

doi:10.1007/s11696-021-01527-9

Cited by 7 publications

(1 citation statement)

References 63 publications

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“…Intrinsic tryptophan fluorescence is a sensitive method to evaluate the modifications in the microenvironment around tryptophan residue. 37,46 It has been frequently used to determine changes in the tertiary structure of proteins. tryptophans are either tightly packed inside and/or located near disulfide bonds, thus quenched.…”

Section: Effect Of Agitation On the Tertiary Structure In The Reduced...mentioning

confidence: 99%

Agitation does not induce fibrillation in reduced hen egg‐white lysozyme at physiological temperature and pH

Malik

Khan

Alhomida

et al. 2023

J of Molecular Recognition

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Several proteins and peptides tend to form an amyloid fibril, causing a range of unrelated diseases, from neurodegenerative to certain types of cancer. In the native state, these proteins are folded and soluble. However, these proteins acquired β‐sheet amyloid fibril due to unfolding and aggregation. The conversion mechanism from well‐folded soluble into amorphous or amyloid fibril is not well understood yet. Here, we induced unfolding and aggregation of hen egg‐white lysozyme (HEWL) by reducing agent dithiothreitol and applied mechanical sheering force by constant shaking (1000 rpm) on the thermostat for 7 days. Our turbidity results showed that reduced HEWL rapidly formed aggregates, and a plateau was attained in nearly 5 h of incubation in both shaking and non‐shaking conditions. The turbidity was lower in the shaking condition than in the non‐shaking condition. The thioflavin T binding and transmission electron micrographs showed that reduced HEWL formed amorphous aggregates in both conditions. Far‐UV circular dichroism results showed that reduced HEWL lost nearly all alpha‐helical structure, and β‐sheet secondary structure was not formed in both conditions. All the spectroscopic and microscopic results showed that reduced HEWL formed amorphous aggregates under both conditions.

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Section: Effect Of Agitation On the Tertiary Structure In The Reduced...mentioning

confidence: 99%