ArticleScientific reports2023
The unusual properties of lactoferrin during its nascent phase.
Article in Scientific reports, 2023. 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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Who cites it
3 citing papers in PubMed.
- Heat-Induced Structural Changes in Lactoferrin for Enhanced Mucoadhesion.ACS applied bio materials · 2025Article
- Lactoferrin and Thioredoxin in Rheumatoid Arthritis Are Associated with Fibrinogen but Not with Other Acute Phase Proteins.International journal of molecular sciences · 2025Article
- Study of pH and Thermodynamic Parameters via Circular Dichroism Spectroscopy of a Recombinant Human Lactoferrin.Molecules (Basel, Switzerland) · 2024Article
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Authors and funding
7 authors.
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Abstract
Lactoferrin, a multifunctional iron-binding protein containing 16 disulfides, is actively studied for its antibacterial and anti-carcinogenic properties. However, scarce information is nowadays available about its oxidative folding starting from the reduced and unfolded status. This study discovers unusual properties when this protein is examined in its reduced molten globule-like conformation. Using kinetic, CD and fluorescence analyses together with mass spectrometry, we found that a few cysteines display astonishing hyper-reactivity toward different thiol reagents. In details, four cysteines (i.e. 668, 64, 512 and 424) display thousands of times higher reactivity toward GSSG but normal against other natural disulfides. The formation of these four mixed-disulfides with glutathione probably represents the first step of its folding in vivo. A widespread low pK
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