ArticleThe European physical journal. E, Soft matter2018
Structural aspects of human lactoferrin in the iron-binding process studied by molecular dynamics and small-angle neutron scattering.
Article in The European physical journal. E, Soft matter, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.Pharmaceutics · 2023Review
- Lactoferrin-The Health-Promoting Properties and Contemporary Application with Genetic Aspects.Foods (Basel, Switzerland) · 2022Review
- Review
- Breast Milk: A Meal Worth Having.Frontiers in nutrition · 2021Review
- Role of Human Milk Bioactives on Infants' Gut and Immune Health.Frontiers in immunology · 2021Review
- Multivalent ions and biomolecules: Attempting a comprehensive perspective.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Review
- Hepcidin and Erythroferrone Correlate with Hepatic Iron Transporters in Rats Supplemented with Multispecies Probiotics.Molecules (Basel, Switzerland) · 2020Article
- β-Lactoglobulin associative interactions: a small-angle scattering study.European biophysics journal : EBJ · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoferrin is a non-heme protein known for its ability to bind tightly Fe(III) ions in various physiological environments. Due to this feature lactoferrin plays an important role in the processes of iron regulation at the cellular level preventing the body from damages produced by high levels of free iron ions. The X-ray crystal structure of human lactoferrin shows that the iron-binding process leads to conformational changes within the protein structure. The present study was addressed to conformation stability of human lactoferrin in solution. Using molecular dynamics simulations, it was shown that Arg121 is the key amino acid in the stabilization of the Fe(III) ion in the N-lobe of human lactoferrin. The small-angle neutron scattering method allowed us to detect the structural differences between the open and closed conformation of human lactoferrin in solution. Our results indicate that the radius of gyration of apolactoferrin appears to be smaller than that of the hololactoferrin, [Formula: see text] Å and [Formula: see text] Å, respectively. The low-resolution three-dimensional models computed for both forms of human lactoferrin in solution also show visible differences, both having a more compact conformation compared to the high-resolution structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.