Fluorescent Neomannosyl Bovine Serum Albumin as Efficient Probe for Mannose Receptor Imaging and MCF-7 Cancer Cell Targeting
Source abstract
Abstract
Robust carbohydrate conjugated fluorescent bovine serum albumin (BSA) as useful tool to study carbohydrate–receptor interactions and in vivo targeting is reported. Amine terminated α-mannoside was attached to fluorescein labeled BSA via diethyl squarate strategy. The surface functionalization and lectin binding specific to fluorescent neomannosyl glycoprotein were confirmed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), surface plasmon resonance (SPR), and microarray imaging. The glycoconjugate was further used to image concanavalin A (ConA), pili of E. coli K12, and lysosomes in MCF-7 cancerous cells successfully, suggesting that this neomannosyl glycoprotein can be used as suitable probe to elucidate carbohydrate–protein interactions, image cancers, and target drug specifically toward tumors.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Glycosylation and Glycoproteins Research · Carbohydrate Chemistry and Synthesis · Hemoglobin structure and function
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
China International Science and Technology Cooperation Base of Food Nutrition/Safety and Medicinal Chemistry, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China
College of Chemical Engineering and Materials Science, Tianjin University of Science and Technology, Tianjin 300457, China
Research Institute of Tsinghua University in Shenzhen, Nanshan District, Shenzhen 518057, China
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, Georgia 30302, United States
Funding
National Natural Science Foundation of China · Shenzhen Science and Technology Innovation Committee · Youth Innovation Research Foundation, Tianjin University of Science and Technology
References (65)
Show source-provided references
1. 10.1039/c3sc50877c10.1039/c3sc50877c ↗
2. 10.1016/j.jmb.2016.07.00510.1016/j.jmb.2016.07.005 ↗
3. 10.1126/science.105982010.1126/science.1059820 ↗
4. 10.1002/cmdc.20150010710.1002/cmdc.201500107 ↗
5. 10.1016/j.cell.2010.11.00810.1016/j.cell.2010.11.008 ↗
6. 10.1016/j.semcdb.2014.12.00110.1016/j.semcdb.2014.12.001 ↗
7. 10.1038/nrm407310.1038/nrm4073 ↗
8. 10.1021/ja210304j10.1021/ja210304j ↗
9. 10.3892/ijo.2015.281810.3892/ijo.2015.2818 ↗
10. 10.1194/jlr.M04913010.1194/jlr.M049130 ↗
11. 10.1111/j.1469-8137.2011.03939.x10.1111/j.1469-8137.2011.03939.x ↗
12. 10.1016/j.abb.2015.02.00710.1016/j.abb.2015.02.007 ↗
13. 10.1093/glycob/cws07010.1093/glycob/cws070 ↗
14. 10.3390/v204101110.3390/v2041011 ↗
15. 10.1080/0785389051000734010.1080/07853890510007340 ↗
16. 10.1046/j.1365-2958.2003.03634.x10.1046/j.1365-2958.2003.03634.x ↗
17. 10.1073/pnas.90.21.985210.1073/pnas.90.21.9852 ↗
18. 10.1002/med.2019610.1002/med.20196 ↗
19. 10.1016/j.drudis.2010.06.00110.1016/j.drudis.2010.06.001 ↗
20. 10.1039/b713011m10.1039/b713011m ↗
21. 10.1039/C2CS35416K10.1039/C2CS35416K ↗
22. 10.1007/s10719-015-9611-910.1007/s10719-015-9611-9 ↗
23. 10.1088/0957-4484/17/1/R0110.1088/0957-4484/17/1/R01 ↗
24. 10.1021/acsami.5b0654110.1021/acsami.5b06541 ↗
25. 10.1039/C6CC06875H10.1039/C6CC06875H ↗
26. 10.1007/s10719-008-9174-010.1007/s10719-008-9174-0 ↗
27. 10.1021/la904488w10.1021/la904488w ↗
28. 10.1146/annurev.bi.65.070196.00230110.1146/annurev.bi.65.070196.002301 ↗
29. 10.1016/j.bmc.2008.03.01710.1016/j.bmc.2008.03.017 ↗
30. 10.1039/C4OB00827H10.1039/C4OB00827H ↗
31. 10.1021/cr000418f10.1021/cr000418f ↗
32. 10.1021/cr500303t10.1021/cr500303t ↗
33. 10.1039/C6RA04273B10.1039/C6RA04273B ↗
34. 10.1016/j.eurpolymj.2013.06.02510.1016/j.eurpolymj.2013.06.025 ↗
35. 10.2174/09298671380507669410.2174/092986713805076694 ↗
36. 10.1016/j.bbagen.2005.12.00110.1016/j.bbagen.2005.12.001 ↗
37. 10.1021/bc500621h10.1021/bc500621h ↗
38. 10.1016/j.bmc.2010.05.04610.1016/j.bmc.2010.05.046 ↗
39. 10.1006/abio.2000.460210.1006/abio.2000.4602 ↗
40. 10.1016/j.trac.2010.05.00510.1016/j.trac.2010.05.005 ↗
41. 10.1016/j.jim.2012.06.00910.1016/j.jim.2012.06.009 ↗
42. 10.1021/la971228b10.1021/la971228b ↗
43. 10.1155/2013/98190210.1155/2013/981902 ↗
44. 10.1515/hc-2017-004910.1515/hc-2017-0049 ↗
45. 10.1016/j.ejmech.2017.10.07010.1016/j.ejmech.2017.10.070 ↗
46. 10.1080/07328303.2017.139057710.1080/07328303.2017.1390577 ↗
47. 10.1016/j.carres.2016.09.01710.1016/j.carres.2016.09.017 ↗
48. 10.1021/acssensors.6b0067910.1021/acssensors.6b00679 ↗
49. 10.1016/j.cclet.2017.10.03210.1016/j.cclet.2017.10.032 ↗
50. 10.1016/j.ejmech.2017.03.05810.1016/j.ejmech.2017.03.058 ↗
51. 10.1021/bm000043810.1021/bm0000438 ↗
52. 10.1021/la304131410.1021/la3041314 ↗
53. 10.1074/jbc.272.10.638810.1074/jbc.272.10.6388 ↗
54. Lotan R. · J. Biol. Chem. · 1975 · 250 · 851810.1016/S0021-9258(19)40790-4 ↗
55. 10.1002/med.2019510.1002/med.20195 ↗
56. 10.1021/ac801065410.1021/ac8010654 ↗
57. 10.1128/JB.183.13.4099-4102.200110.1128/JB.183.13.4099-4102.2001 ↗
58. Soto G. E. · J. Bacteriol. · 1999 · 181 · 105910.1128/JB.181.4.1059-1071.1999 ↗
59. 10.1016/j.tetlet.2008.12.02910.1016/j.tetlet.2008.12.029 ↗
60. 10.1007/s11051-013-1819-710.1007/s11051-013-1819-7 ↗
61. 10.1007/s11468-011-9307-310.1007/s11468-011-9307-3 ↗
62. 10.1021/am401712610.1021/am4017126 ↗
63. 10.1016/j.ejmech.2016.05.06910.1016/j.ejmech.2016.05.069 ↗
64. 10.1080/07328303.2017.140361310.1080/07328303.2017.1403613 ↗
65. 10.1074/jbc.M115.64288410.1074/jbc.M115.642884 ↗