CoChat
Sign Up
Cited by 21

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A biomimetic magnetosome: formation of iron oxide within carboxylic acid terminated polymersomes

Bain, Jennifer, Legge, Christopher J., Beattie, Deborah L., Sahota, Annie, Dirks, Catherine, Lovett, Joseph R., Staniland, Sarah S.·2019·Nanoscale
DOI 10.1039/c9nr00498j
Open this paper in CoChat — free account

Abstract

Bioinspired macromolecules can aid nucleation and crystallisation of minerals by mirroring processes observed in nature.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1039/c9nr00498j

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Fig. 1 Schematic of natural and synthetic vesicle membranes (blue = hydrophilic membrane lea fl et, red = hydrophobic membrane lea fl et) representing, (a) the bacterial magnetosome in which iron is recruited into the core of the magnetosome using iron transporters, which also acts an antiporter pumping out internal protons. The e ffl ux of protons causes a pH increase resulting in the precipitation the magnetite crystal. The magnetite nucleation protein Mms6 (inset bottom left) which accumulates iron ions on the acidic amino acids on the inner lumen of the magnetosome. (b) Chemical composition of PEG-PHPMA and PMPC-PHPMA polymer which represent the hydrophilic (blue) and hydrophobic (red) lea fl ets of the vesicles, which features a carboxylic acid group on the PMPC monomer to mimic the iron ion binding/mineral nucleating sites of the Mms6 protein. The lighting represents electroporation to mimic the protein iron transporter, while the insert shows how the acidic end groups on PMPC mimic Mms6.
Fig. 1 Schematic of natural and synthetic vesicle membranes (blue = hydrophilic membrane lea fl et, red = hydrophobic membrane lea fl et) representing, (a) the bacterial magnetosome in which iron is recruited into the core of the magnetosome using iron transporters, which also acts an antiporter pumping out internal protons. The e ffl ux of protons causes a pH increase resulting in the precipitation the magnetite crystal. The magnetite nucleation protein Mms6 (inset bottom left) which accumulates iron ions on the acidic amino acids on the inner lumen of the magnetosome. (b) Chemical composition of PEG-PHPMA and PMPC-PHPMA polymer which represent the hydrophilic (blue) and hydrophobic (red) lea fl ets of the vesicles, which features a carboxylic acid group on the PMPC monomer to mimic the iron ion binding/mineral nucleating sites of the Mms6 protein. The lighting represents electroporation to mimic the protein iron transporter, while the insert shows how the acidic end groups on PMPC mimic Mms6.CC-BY · From the PDF
Fig. 2 Poly(ethylene glycol)-poly(2-hydroxypropyl methacrylate)/poly (2-(methacryloyloxy)ethyl phosphorylcholine)-poly(2-hydroxypropyl methacrylate) (PEG + PMPC)-PHPMA polymersomes are prepared by chain extension of a binary mixture of PEG113 and PMPC28 macro-CTAs via reversible addition -fragmentation chain transfer (RAFT) aqueous dispersion polymerisation of 2-hydroxypropyl methacrylate (HPMA). 45
Fig. 2 Poly(ethylene glycol)-poly(2-hydroxypropyl methacrylate)/poly (2-(methacryloyloxy)ethyl phosphorylcholine)-poly(2-hydroxypropyl methacrylate) (PEG + PMPC)-PHPMA polymersomes are prepared by chain extension of a binary mixture of PEG113 and PMPC28 macro-CTAs via reversible addition -fragmentation chain transfer (RAFT) aqueous dispersion polymerisation of 2-hydroxypropyl methacrylate (HPMA). 45CC-BY · From the PDF
Fig. 3 (a) Negatively stained TEM images of PMM28 polymersomes, (b) cryo-TEM image of PMM28 to show hydrated size is consistent with (a). (c) TEM grainsizing of the polymersome sample.
Fig. 3 (a) Negatively stained TEM images of PMM28 polymersomes, (b) cryo-TEM image of PMM28 to show hydrated size is consistent with (a). (c) TEM grainsizing of the polymersome sample.CC-BY · From the PDF
Fig. 4 Unstained TEM images of (a) PMM28Fe. The PMM28 sample was soaked in NaOH (10 mM) before electroporation at 750 V (5 pulses) in the presence of excess FeCl2·4H2O. The polymersomes show dark electron dense cores, attributed to the precipitation of magnetic iron oxide.
Fig. 4 Unstained TEM images of (a) PMM28Fe. The PMM28 sample was soaked in NaOH (10 mM) before electroporation at 750 V (5 pulses) in the presence of excess FeCl2·4H2O. The polymersomes show dark electron dense cores, attributed to the precipitation of magnetic iron oxide.CC-BY · From the PDF
Fig. 5 (a) Unstained TEM image of electroporated PMM28Fe polymersomes showing precipitation on the outer lea fl et of the polymersome as well as in the vesicle core. (b) A selected area electron di ff raction image of the same electroporated polymersome con fi rming the presence of a crystalline substance within the polymersome. (c) Cryo-EM micrograph of PEO-PBD polymersomes from the fi rst reported use of the electroporation method 29 and (d) show comparison of use of the electroporation method on PMOXA-DMS-MOXA tri-block polymersomes. 30
Fig. 5 (a) Unstained TEM image of electroporated PMM28Fe polymersomes showing precipitation on the outer lea fl et of the polymersome as well as in the vesicle core. (b) A selected area electron di ff raction image of the same electroporated polymersome con fi rming the presence of a crystalline substance within the polymersome. (c) Cryo-EM micrograph of PEO-PBD polymersomes from the fi rst reported use of the electroporation method 29 and (d) show comparison of use of the electroporation method on PMOXA-DMS-MOXA tri-block polymersomes. 30CC-BY · From the PDF
Fig. 6 Temperature increase vs. time curve obtained during magnetic hyperthermic heating of a 0.2% w/v aqueous dispersion of PMM28Fe polymersomes (0.11 mg ml -1 of iron). A temperature increase of 6 °C is observed over a period of 10 minutes (600 s).
Fig. 6 Temperature increase vs. time curve obtained during magnetic hyperthermic heating of a 0.2% w/v aqueous dispersion of PMM28Fe polymersomes (0.11 mg ml -1 of iron). A temperature increase of 6 °C is observed over a period of 10 minutes (600 s).CC-BY · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 50

  1. Kirschvink, 1992, Proc. Natl. Acad. Sci. U. S. A., 89, 7683, 10.1073/pnas.89.16.7683 · DOI
  2. J. L. Kirschvink and J. W.Hagadorn , 10 A grand unified theory of biomineralization, The Biomineralisation of Nano-and Micro-Structures , Wiley-VCH Verlag GmbH , Weinheim, Germany , 2000 , pp. 139–150
  3. Skinner, 2003, Treatise Geochem., 8, 117
  4. S. Mann , Biomineralization: Principles and Concepts in Bioinorganic Materials Chemistry , 2001 · DOI
  5. Nies, 2011, Mol. Microbiol., 82, 792, 10.1111/j.1365-2958.2011.07864.x · DOI
  6. Komeili, 2004, Proc. Natl. Acad. Sci. U. S. A., 101, 3839, 10.1073/pnas.0400391101 · DOI
  7. Weiner, 1991, Trends Biochem. Sci., 16, 252, 10.1016/0968-0004(91)90098-G · DOI
  8. Sodek, 2000, Crit. Rev. Oral Biol. Med., 11, 279, 10.1177/10454411000110030101 · DOI
  9. Jiang, 2017, Nat. Commun., 8, 15066, 10.1038/ncomms15066 · DOI
  10. Arakaki, 2003, J. Biol. Chem., 278, 8745, 10.1074/jbc.M211729200 · DOI
  11. Amemiya, 2007, Biomaterials, 28, 5381, 10.1016/j.biomaterials.2007.07.051 · DOI
  12. Staniland, 2016, Biochem. Soc. Trans., 44, 883, 10.1042/BST20160057 · DOI
  13. Bird, 2016, RSC Adv., 6, 7356, 10.1039/C5RA16469A · DOI
  14. Kashyap, 2014, ACS Nano, 8, 9097, 10.1021/nn502551y · DOI
  15. Wang, 2012, Biomacromolecules, 13, 98, 10.1021/bm201278u · DOI
  16. Rawlings, 2016, Chem. – Eur. J., 22, 7885, 10.1002/chem.201600322 · DOI
  17. Murat, 2012, Mol. Microbiol., 85, 684, 10.1111/j.1365-2958.2012.08132.x · DOI
  18. Nudelman, 2014, Front. Microbiol., 5, 9, 10.3389/fmicb.2014.00009 · DOI
  19. Janib, 2010, Adv. Drug Delivery Rev., 62, 1052, 10.1016/j.addr.2010.08.004 · DOI
  20. Guan, 2015, Nanomedicine, 10, 2757, 10.2217/nnm.15.110 · DOI
  21. Schmaljohann, 2006, Adv. Drug Delivery Rev., 58, 1655, 10.1016/j.addr.2006.09.020 · DOI · Paper page
  22. Kallumadil, 2009, J. Magn. Magn. Mater., 321, 1509, 10.1016/j.jmmm.2009.02.075 · DOI
  23. Hergt, 2005, J. Magn. Magn. Mater., 293, 80, 10.1016/j.jmmm.2005.01.047 · DOI
  24. Plan Sangnier, 2018, J. Controlled Release, 279, 271, 10.1016/j.jconrel.2018.04.036 · DOI
  25. Hergt, 2006, J. Phys.: Condens. Matter, 18, S2919
  26. Ludwig, 2014, Nanoscale Res. Lett., 9, 602, 10.1186/1556-276X-9-602 · DOI
  27. Pankhurst, 2003, J. Phys. D: Appl. Phys., 36, R167, 10.1088/0022-3727/36/13/201 · DOI
  28. Kumar, 2011, Adv. Drug Delivery Rev., 63, 789, 10.1016/j.addr.2011.03.008 · DOI
  29. Bain, 2015, Sci. Rep., 5, 14311, 10.1038/srep14311 · DOI · Paper page
  30. Bain, 2015, Polymers, 7, 1529, 10.3390/polym7121529 · DOI
  31. Weaver, 1993, J. Cell. Biochem., 51, 426, 10.1002/jcb.2400510407 · DOI
  32. Gehl, 2003, Acta Physiol. Scand., 177, 437, 10.1046/j.1365-201X.2003.01093.x · DOI
  33. Escoffre, 2009, Mol. Biotechnol., 41, 286, 10.1007/s12033-008-9121-0 · DOI
  34. Tieleman, 2004, BMC Biochem., 5, 10, 10.1186/1471-2091-5-10 · DOI
  35. Wang, 2012, Angew. Chem., Int. Ed., 51, 11122, 10.1002/anie.201204169 · DOI
  36. Weaver, 1996, Bioelectrochem. Bioenerg., 41, 135, 10.1016/S0302-4598(96)05062-3 · DOI
  37. Ning, 2016, ACS Macro Lett., 5, 311, 10.1021/acsmacrolett.6b00022 · DOI
  38. Blanazs, 2011, Soft Matter, 7, 6399, 10.1039/c1sm05771e · DOI
  39. Discher, 2002, Science, 297, 967, 10.1126/science.1074972 · DOI
  40. Antonietti, 2003, Adv. Mater., 15, 1323, 10.1002/adma.200300010 · DOI
  41. Zhang, 1998, Polym. Adv. Technol., 9, 677, 10.1002/(SICI)1099-1581(1998100)9:10/11<677::AID-PAT845>3.0.CO;2-# · DOI
  42. Blanazs, 2009, Macromol. Rapid Commun., 30, 267, 10.1002/marc.200800713 · DOI · Paper page
  43. Zhang, 2012, Macromolecules, 45, 4075, 10.1021/ma300596f · DOI
  44. Warren, 2014, J. Am. Chem. Soc., 136, 10174, 10.1021/ja502843f · DOI
  45. Canning, 2016, Macromolecules, 49, 1985, 10.1021/acs.macromol.5b02602 · DOI
  46. Sugihara, 2011, J. Am. Chem. Soc., 133, 15707, 10.1021/ja205887v · DOI
  47. Gonzato, 2014, J. Am. Chem. Soc., 136, 11100, 10.1021/ja505406s · DOI
  48. Lovett, 2015, Angew. Chem., Int. Ed., 54, 1279, 10.1002/anie.201409799 · DOI
  49. Chambon, 2012, Macromolecules, 45, 5081, 10.1021/ma300816m · DOI
  50. Wildeboer, 2014, J. Phys. D: Appl. Phys., 47, 495003, 10.1088/0022-3727/47/49/495003 · DOI

Cited by

Sorted by citations

See all 21

Metadata

Authors
Bain, J., Legge, C. J., Beattie, D. L., Sahota, A., Dirks, C., Lovett, J. R., & Staniland, S. S.
Affiliations
Department of Chemistry
ORCID
Staniland, Sarah S.
Venue
Nanoscale
Publisher
Royal Society of Chemistry (RSC)
Published
2019
Volume
11
Issue
24
Pages
11617-11625
ISSN
  • 2040-3364
  • 2040-3372
DOI
10.1039/c9nr00498j
Cited by
21
References
1
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor, 157 d)
Funders
Engineering and Physical Sciences Research Council (EP/I032355/2)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: A biomimetic magnetosome: formation of iron oxide within carboxylic acid terminated polymersomes. https://app.cochat.ai/papers/10.1039/c9nr00498j
The paper
Bain, J., Legge, C. J., Beattie, D. L., Sahota, A., Dirks, C., Lovett, J. R., & Staniland, S. S. (2019). A biomimetic magnetosome: formation of iron oxide within carboxylic acid terminated polymersomes. Nanoscale. https://doi.org/10.1039/c9nr00498j