Gold Nanoparticle-Based Facile Detection of Human Serum Albumin and Its Application as an INHIBIT Logic Gate
Source abstract
Abstract
In this work, a facile colorimetric method is developed for quantitative detection of human serum albumin (HSA) based on the antiaggregation effect of gold nanoparticles (Au NPs) in the presence of HSA. The citrate-capped Au NPs undergo a color change from red to blue when melamine is added as a cross-linker to induce the aggregation of the NPs. Such an aggregation is efficiently suppressed upon the adsorption of HSA on the particle surface. This method provides the advantages of simplicity and cost-efficiency for quantitative detection of HSA with a detection limit of ∼1.4 nM by monitoring the colorimetric changes of the Au NPs with UV-vis spectroscopy. In addition, this approach shows good selectivity for HSA over various amino acids, peptides, and proteins and is qualified for detection of HSA in a biological sample. Such an antiaggregation effect can be further extended to fabricate an INHIBIT logic gate by using HSA and melamine as inputs and the color changes of Au NPs as outputs, which may have application potentials in point-of-care medical diagnosis.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Protein Interaction Studies and Fluorescence Analysis · Gold and Silver Nanoparticles Synthesis and Applications · Advanced biosensing and bioanalysis techniques
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, People’s Republic of China
Funding
Ministry of Science and Technology of the People's Republic of China · China Postdoctoral Science Foundation · National Natural Science Foundation of China
References (53)
Show source-provided references
1. Westermeier R. · Biosci. Rep. · 2005 · 25 · 1910.1007/s10540-005-2845-1 ↗
2. Zhang Y. · Adv. Mater. · 2013 · 25 · 380210.1002/adma.201301334 ↗
3. Doumas B. T. · Clin. Chim. Acta · 1997 · 258 · 310.1016/S0009-8981(96)06446-7 ↗
4. Arques S. · J. Card. Failure · 2011 · 17 · 45110.1016/j.cardfail.2011.02.010 ↗
5. Fanali G. · Mol. Aspects Med. · 2012 · 33 · 20910.1016/j.mam.2011.12.002 ↗
6. Tu M. C. · Biosens. Bioelectron. · 2012 · 34 · 28610.1016/j.bios.2011.11.035 ↗
7. Caballero D. · Anal. Chim. Acta · 2012 · 720 · 4310.1016/j.aca.2012.01.031 ↗
8. Contois J. H. · Clin. Chim. Acta · 2006 · 367 · 15010.1016/j.cca.2005.12.002 ↗
9. Singh R. · Clin. Chem. · 2007 · 53 · 54010.1373/clinchem.2006.078832 ↗
10. Chen X. T. · Talanta · 2010 · 80 · 195210.1016/j.talanta.2009.10.053 ↗
11. Wang X. H. · Chem. Commun. · 2011 · 47 · 812710.1039/c1cc12429c ↗
12. Sun H. X. · Analyst · 2014 · 139 · 58110.1039/C3AN01929B ↗
13. Chai F. · ACS Appl. Mater. Interfaces · 2010 · 2 · 146610.1021/am100107k ↗
14. Yanga C. · Biosens. Bioelectron. · 2011 · 26 · 272410.1016/j.bios.2010.09.032 ↗
15. Saha K. · Chem. Rev. · 2012 · 112 · 273910.1021/cr2001178 ↗
16. He K. · J. Nanopart. Res. · 2013 · 15
17. Si S. · J. Phys. Chem. C · 2007 · 111 · 124810.1021/jp066303i ↗
18. Lin M. H. · Adv. Mater. · 2013 · 25 · 349010.1002/adma.201301333 ↗
19. Guo L. Q. · Talanta · 2010 · 82 · 165410.1016/j.talanta.2010.07.035 ↗
20. Chi H. · Analyst · 2010 · 135 · 107010.1039/c000285b ↗
21. Du J. J. · Chem. Commun. · 2013 · 49 · 419610.1039/C2CC36955A ↗
22. Jiang Q. · Small · 2013 · 9 · 101610.1002/smll.201201760 ↗
23. Deng H. H. · Analyst · 2013 · 138 · 667710.1039/c3an01520c ↗
24. Huang Z. Z. · Nanoscale · 2014 · 6 · 830010.1039/C4NR01615G ↗
25. Ji X. H. · J. Am. Chem. Soc. · 2007 · 129 · 1393910.1021/ja074447k ↗
26. Vangala K. · J. Phys. Chem. C · 2012 · 116 · 364510.1021/jp2107318 ↗
27. Qu Z. Y. · Bioconjugate Chem. · 2014 · 25 · 37010.1021/bc400530s ↗
28. Zhou Y. · Analyst · 2014 · 139 · 312210.1039/C4AN00487F ↗
29. Liu Y. · J. Am. Chem. Soc. · 2011 · 133 · 66010.1021/ja107086y ↗
30. Wang Y. · Talanta · 2014 · 119 · 32010.1016/j.talanta.2013.11.026 ↗
31. Dominguez-Medina S. · Langmuir · 2012 · 28 · 913110.1021/la3005213 ↗
32. Templeton A. C. · J. Phys. Chem. B · 2000 · 104 · 56410.1021/jp991889c ↗
33. Yan H. · J. Mol. Struct. · 2010 · 967 · 6110.1016/j.molstruc.2009.12.039 ↗
34. Dominguez-Medina S. · ACS Sustainable Chem. Eng. · 2013 · 1 · 83310.1021/sc400042h ↗
35. Vangala K. · J. Phys. Chem. C · 2013 · 117 · 136610.1021/jp310085u ↗
36. Adhikari M. D. · RSC Adv. · 2012 · 2 · 178210.1039/C1RA01023A ↗
37. Long G. L. · Anal. Chem. · 1983 · 55 · 712
38. Ooka A. A. · Biospectroscopy · 1999 · 5 · 910.1002/(SICI)1520-6343(1999)5:1<9::AID-BSPY3>3.0.CO;2-T ↗
39. Siriwardana K. · Langmuir · 2013 · 29 · 1099010.1021/la402239h ↗
40. Kah J. C. Y. · ACS Nano · 2012 · 6 · 673010.1021/nn301389c ↗
41. Liu W. H. · J. Am. Chem. Soc. · 2007 · 129 · 1453010.1021/ja073790m ↗
42. Taladriz-Blanco P. · Langmuir · 2013 · 29 · 806110.1021/la4014762 ↗
43. Requejo R. · FEBS J. · 2010 · 277 · 146510.1111/j.1742-4658.2010.07576.x ↗
44. Tanaka N. · Biochim. Biophys. Acta · 1997 · 1338 · 1310.1016/S0167-4838(96)00175-6 ↗
45. Miller W. G. · Clin. Chem. · 2009 · 55 · 2410.1373/clinchem.2008.106567 ↗
46. Kozhevnikov A. D. · Arch. Int. Med. · 2002 · 162 · 35610.1001/archinte.162.3.356 ↗
47. Clavant S. P. · J. Lab. Clin. Med. · 2003 · 142 · 37210.1016/S0022-2143(03)00150-1 ↗
48. Bito R. · Am. J. Physiol. Cell Physiol. · 2005 · 289 · 53110.1152/ajpcell.00431.2004 ↗
49. Sinha S. S. · J. Phys. Chem. B · 2008 · 112 · 488410.1021/jp709809b ↗
50. Rezaei-Tavirani1 M. · J. Biochem. Mol. Biol. · 2006 · 39 · 530
51. Holm N. K. · Biochim. Biophys. Acta · 2007 · 1774 · 112810.1016/j.bbapap.2007.06.008 ↗
52. Fleischer C. C. · J. Phys. Chem. B · 2014 · 118 · 1401710.1021/jp502624n ↗
53. Fleischer C. C. · Acc. Chem. Res. · 2014 · 47 · 265110.1021/ar500190q ↗