Facile Synthesis of Magnetic Mesoporous Hollow Carbon Microspheres for Rapid Capture of Low-Concentration Peptides
Source abstract
Abstract
Mesoporous and hollow carbon microspheres embedded with magnetic nanoparticles (denoted as MHM) were prepared via a facile self-sacrificial method for rapid capture of low-abundant peptides from complex biological samples. The morphology, structure, surface property, and magnetism were well-characterized. The hollow magnetic carbon microspheres have a saturation magnetization value of 130.2 emu g(-1) at room temperature and a Brunauer-Emmett-Teller specific surface area of 48.8 m(2) g(-1) with an average pore size of 9.2 nm for the mesoporous carbon shell. The effectiveness of these MHM affinity microspheres for capture of low-concentration peptides was evaluated by standard peptides, complex protein digests, and real biological samples. These multifunctional hollow carbon microspheres can realize rapid capture and convenient separation of low-concentration peptides. They were validated to have better performance than magnetic mesoporous silica and commercial peptide-enrichment products. In addition, they can be easily recycled and present excellent reusability. Therefore, it is expected that this work may provide a promising tool for high-throughput discovery of peptide biomarkers from biological samples for disease diagnosis and other biomedical applications.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Graphene and Nanomaterials Applications · Nanoparticle-Based Drug Delivery
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania 16802, United States
Funding
National Institutes of Health
References (53)
Show source-provided references
1. Qiu L. · Nat. Commun. · 2012 · 3 · 124110.1038/ncomms2251 ↗
2. Cargnello M. · J. Am. Chem. Soc. · 2012 · 134 · 1176010.1021/ja304398b ↗
3. Zhu M. · Nanoscale · 2011 · 3 · 274810.1039/c1nr10165j ↗
4. Merlet C. · Nat. Mater. · 2012 · 11 · 30610.1038/nmat3260 ↗
5. Ganesan R. · Angew. Chem., Int. Ed. · 2005 · 44 · 655710.1002/anie.200501272 ↗
6. Zhang S. · Chem. Mater. · 2010 · 22 · 343310.1021/cm1002274 ↗
7. Cheng G. · Chem. Commun. · 2012 · 48 · 1024010.1039/c2cc35483g ↗
8. Liu Z. · Mater. Today · 2011 · 14 · 31610.1016/S1369-7021(11)70161-4 ↗
9. Sahoo N. G. · Chem. Commun. · 2011 · 47 · 523510.1039/c1cc00075f ↗
10. Feng L. · Adv. Mater. · 2012 · 25 · 16810.1002/adma.201203229 ↗
11. Cheng G. · J. Mater. Chem. · 2012 · 22 · 2199810.1039/c2jm33695b ↗
12. Li H. · Chem. Commun. · 2011 · 47 · 96110.1039/C0CC04326E ↗
13. Ray S. · Proteomics · 2011 · 11 · 213910.1002/pmic.201000460 ↗
14. Beretta L. · Nat. Methods · 2007 · 4 · 78510.1038/nmeth1007-785 ↗
15. Felipe C. D. · Nature · 1998 · 392 · 39410.1038/32904 ↗
16. Coll A. P. · Cell · 2007 · 129 · 25110.1016/j.cell.2007.04.001 ↗
17. Doerr A. · Nat. Methods · 2008 · 5 · 85810.1038/nmeth1008-858b ↗
18. Swami M. · Nat. Rev. Cancer · 2010 · 10 · 59710.1038/nrc2922 ↗
19. Sauer S. · Nat. Rev. Microbiol. · 2010 · 8 · 7410.1038/nrmicro2243 ↗
20. Yates J. R. · Nat. Methods · 2011 · 8 · 63310.1038/nmeth.1659 ↗
21. Xiong H. M. · Angew. Chem., Int. Ed. · 2008 · 47 · 420410.1002/anie.200705942 ↗
22. Chen H. · Proteomics · 2008 · 8 · 277810.1002/pmic.200700892 ↗
23. Gu Z.-Y. · Chem. Commun. · 2011 · 47 · 478710.1039/c1cc10579e ↗
24. Li Y. · Chem. Soc. Rev. · 2013 · 42 · 851710.1039/c3cs60156k ↗
25. Zhao M. · ACS Appl. Mater. Interfaces · 2013 · 5 · 1310410.1021/am4041042 ↗
26. Qin H. · Angew. Chem., Int. Ed. · 2011 · 50 · 1221810.1002/anie.201103666 ↗
27. Landázuri N. · Small · 2013 · 9 · 401710.1002/smll.201300570 ↗
28. Woo E. · J. Mater. Chem. · 2010 · 20 · 151110.1039/B918682D ↗
29. Liu Y. · ACS Appl. Mater. Interfaces · 2012 · 4 · 491310.1021/am301239u ↗
30. Dui J. · ACS Appl. Mater. Interfaces · 2013 · 5 · 1008110.1021/am402656t ↗
31. Cheng G. · Chem. Commun. · 2011 · 47 · 573210.1039/c1cc10533g ↗
32. Cheng G. · ACS Appl. Mater. Interfaces · 2013 · 5 · 318210.1021/am400191u ↗
33. Wu Z. · Adv. Mater. · 2011 · 24 · 48510.1002/adma.201103789 ↗
34. Liu J. · Angew. Chem., Int. Ed. · 2009 · 48 · 587510.1002/anie.200901566 ↗
35. Cheng G. · Anal. Bioanal. Chem. · 2012 · 404 · 76310.1007/s00216-012-6150-0 ↗
36. Liu R. · Angew. Chem., Int. Ed. · 2011 · 50 · 679910.1002/anie.201102070 ↗
37. Cheng G. · Chem.—Eur. J. · 2012 · 18 · 201410.1002/chem.201103328 ↗
38. Mandal M. · J. Colloid Interface Sci. · 2005 · 286 · 18710.1016/j.jcis.2005.01.013 ↗
39. Kyeongse S. · Nanotechnology · 2012 · 23 · 50540110.1088/0957-4484/23/50/505401 ↗
40. Thakur V. K. · J. Mater. Chem. · 2012 · 22 · 595110.1039/c2jm15665b ↗
41. Zhang L.-W. · Adv. Funct. Mater. · 2008 · 18 · 218010.1002/adfm.200701478 ↗
42. Liu Q. · Macromol. Biosci. · 2011 · 11 · 122710.1002/mabi.201100061 ↗
43. Martin M. · J. Mater. Chem. B · 2013 · 2 · 73910.1039/C3TB21171A ↗
44. Yan Y. · Chem. Commun. · 2013 · 49 · 505510.1039/c3cc41330f ↗
45. Zhang M. · J. Mater. Chem. · 2010 · 20 · 1069610.1039/c0jm01336f ↗
46. Pierotti R. · Pure Appl. Chem. · 1985 · 57 · 60310.1351/pac198557040603 ↗
47. Ai K. · Adv. Mater. · 2013 · 25 · 99810.1002/adma.201203923 ↗
48. Kim O.-H. · Nat. Commun. · 2013 · 4 · 247310.1038/ncomms3473 ↗
49. Pulko I. · Chem.—Eur. J. · 2010 · 16 · 235010.1002/chem.200903043 ↗
50. Du J. · ACS Nano · 2010 · 5 · 59010.1021/nn102767d ↗
51. Liu S. · Angew. Chem., Int. Ed. · 2010 · 49 · 755710.1002/anie.201003602 ↗
52. Casado-Vela J. · Expert Rev. Proteomics · 2011 · 8 · 34710.1586/epr.11.26 ↗
53. Chen Y.-T. · J. Proteomics · 2012 · 75 · 352910.1016/j.jprot.2011.12.031 ↗