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The Biochemical journal1995; 307 ( Pt 1)(Pt 1); 253-256; doi: 10.1042/bj3070253

Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation.

Abstract: The NMR relaxation technique was used to investigate the permeation of molecules into the cavity of ferritin. Spin-lattice relaxation times in the rotating frame of various probe molecules were measured for solutions of recombinant horse L-apoferritin without iron and horse spleen apoferritin with very small amounts of ferric ions. The results show that molecules larger than the size of the ferritin channels can pass through the channels into the ferritin interior, and that the maximum size of molecules for the permeation is smaller than maltotriose.
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Publication Date: 1995-04-01 PubMed ID: 7717984PubMed Central: PMC1136770DOI: 10.1042/bj3070253Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research study uses nuclear magnetic resonance (NMR) relaxation methodology to uncover how small molecules can permeate the cavity of a protein, ferritin. It was discovered that despite their size, some molecules can pass through the ferritin channels, but the size limit for these molecules is smaller than maltotriose.

Methodology

  • The researchers used a technique called spin-lattice relaxation in the rotating frame. This is a type of NMR technique that measures how quickly the spins of protons return to equilibrium following a disturbance, a process known as relaxation.
  • They performed this measurement on various probe molecules in solutions of two types of apoferritin: one obtained from recombinant horse L-apoferritin without iron and the other from horse spleen apoferritin containing very small amounts of ferric ions. Apoferritin is a protein that stores iron in a non-toxic form and releases it in a controlled manner.

Findings

  • The results shed light on how molecules larger than the size of ferritin channels manage to enter the cavity or interior of ferritin.
  • They found that the maximum size of the molecules that can permeate the ferritin structure is smaller than that of maltotriose. Maltotriose is a trisaccharide, a carbohydrate composed of three sugar units.

Significance

  • The research provides important insights into the behaviour and characteristics of the ferritin protein. This information can potentially enhance our understanding of iron storage and metabolism inside cells.
  • The findings also have implications for more targeted drug delivery methods where small molecule drugs can be specifically designed to permeate the cavities of proteins like ferritin.

Cite This Article

APA
Yang D, Nagayama K. (1995). Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation. Biochem J, 307 ( Pt 1)(Pt 1), 253-256. https://doi.org/10.1042/bj3070253

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 307 ( Pt 1)
Issue: Pt 1
Pages: 253-256

Researcher Affiliations

Yang, D
  • Nagayama Protein Array Project, ERATO, JRDC, Tsukuba Research Consortium, Japan.
Nagayama, K

    MeSH Terms

    • Animals
    • Apoferritins / chemistry
    • Carbohydrate Sequence
    • Dimethyl Sulfoxide / metabolism
    • Ferritins / chemistry
    • Glucose / metabolism
    • Horses
    • Iron / metabolism
    • Magnetic Resonance Spectroscopy
    • Maltose / analogs & derivatives
    • Maltose / metabolism
    • Molecular Sequence Data
    • Molecular Weight
    • Oligosaccharides / metabolism
    • Polyethylene Glycols / metabolism
    • Protein Conformation
    • Recombinant Proteins / chemistry
    • Spleen / chemistry
    • Trisaccharides / metabolism
    • Water / metabolism

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    This article includes 14 references
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    Citations

    This article has been cited 9 times.
    1. Muhoberac BB, Vidal R. Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration. Front Neurosci 2019;13:1195.
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    2. Zhen Z, Tang W, Todd T, Xie J. Ferritins as nanoplatforms for imaging and drug delivery. Expert Opin Drug Deliv 2014 Dec;11(12):1913-22.
      doi: 10.1517/17425247.2014.941354pubmed: 25070839google scholar: lookup
    3. Huard DJ, Kane KM, Tezcan FA. Re-engineering protein interfaces yields copper-inducible ferritin cage assembly. Nat Chem Biol 2013 Mar;9(3):169-76.
      doi: 10.1038/nchembio.1163pubmed: 23340339google scholar: lookup
    4. Barnés CM, Theil EC, Raymond KN. Iron uptake in ferritin is blocked by binding of [Cr(TREN)(H(2)O)(OH)](2+), a slow dissociating model for [Fe(H(2)O)(6)](2+). Proc Natl Acad Sci U S A 2002 Apr 16;99(8):5195-200.
      doi: 10.1073/pnas.032089399pubmed: 11959967google scholar: lookup
    5. Yang X, Arosio P, Chasteen ND. Molecular diffusion into ferritin: pathways, temperature dependence, incubation time, and concentration effects. Biophys J 2000 Apr;78(4):2049-59.
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    6. Yang X, Chasteen ND. Molecular diffusion into horse spleen ferritin: a nitroxide radical spin probe study. Biophys J 1996 Sep;71(3):1587-95.
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    7. Levi S, Santambrogio P, Corsi B, Cozzi A, Arosio P. Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation. Biochem J 1996 Jul 15;317 ( Pt 2)(Pt 2):467-73.
      doi: 10.1042/bj3170467pubmed: 8713073google scholar: lookup
    8. Vekilov PG, Verma L, Palmer JC, Chakrabarti R, Warzecha M. The pathway from the solution to the steps. J Cryst Growth 2022 Dec 1;599.
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    9. Cassioli ML, Fay M, Turyanska L, Bradshaw TD, Thomas NR, Pordea A. Encapsulation of copper phenanthroline within horse spleen apoferritin: characterisation, cytotoxic activity and ability to retain temozolomide. RSC Adv 2024 Apr 25;14(20):14008-14016.
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