ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2022
The influence of cations on α-lactalbumin amyloid aggregation.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 10 citations in OpenAlex.
- Determination of Theophylline Across Biological, Environmental and Food Matrices Using Liquid-Phase Microextraction Coupled with LC-MS/MS.Molecules (Basel, Switzerland) · 2025Article
- Multispectroscopic and computational insights into amyloid fibril formation of alpha lactalbumin induced by sodium hexametaphosphate.Scientific reports · 2024Article
- Influence of divalent metal cations on α-lactalbumin fibril formation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
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6 authors at 2 institutions in 2 countries.
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Abstract
There is limited knowledge regarding α-lactalbumin amyloid aggregation and its mechanism. We examined the formation of α-lactalbumin amyloid fibrils (α-LAF) in the presence of cations (Mg<sup>2+</sup>, Ca<sup>2+</sup>, Na<sup>+</sup>, K<sup>+</sup>, NH<sub>4</sub><sup>+</sup>, and Cs<sup>+</sup>) in the form of chloride salts at two concentrations. We have shown that studied cations affect the conformation of α-lactalbumin, the kinetics of its amyloid formation, morphology, and secondary structure of α-LAF in a different manner. The higher salts concentration significantly accelerated the aggregation process. Both salt concentrations stabilized α-lactalbumin's secondary structure. However, the presence of divalent cations resulted in shorter fibrils with less β-sheet content. Moreover, strongly hydrated Mg<sup>2+</sup> significantly altered α-lactalbumin's tertiary structure, followed by Na<sup>+</sup>, NH<sub>4</sub><sup>+</sup>, K<sup>+</sup>, and weakly hydrated Cs<sup>+</sup>. On the other hand, Ca<sup>2+</sup>, despite being also strongly hydrated, stabilized the tertiary structure, supposedly due to its high affinity towards α-lactalbumin. Yet, Ca<sup>2+</sup> was not able to inhibit α-lactalbumin amyloid aggregation.
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