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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | You, Fei Yin, Guangfu Pu, Ximing Li, Yucan Hu, Yang Huang, Zhongbin Liao, Xiaoming Yao, Yadong Chen, Xianchun |
| Description | Author Affiliation: You F ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Yin G ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China. Electronic address: nic0700@scu.edu.cn.); Pu X ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Li Y ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Hu Y ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Huang Z ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Liao X ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Yao Y ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.); Chen X ( College of Materials Science and Engineering, Sichuan University, Chengdu 610065, PR China.) |
| Abstract | Functionalization of inorganic nanoparticles (NPs) play an important role in biomedical applications. A proper functionalization of NPs can improve biocompatibility, avoid a loss of bioactivity, and further endow NPs with unique performances. Modification with vairous specific binding biomolecules from random biological libraries has been explored. In this work, two 7-mer peptides with sequences of HYIDFRW and TVNFKLY were selected from a phage display random peptide library by using ferromagnetic NPs as targets, and were verified to display strong binding affinity to Fe3O4 NPs. Fourier transform infrared spectrometry, fluorescence microscopy, thermal analysis and X-ray photoelectron spectroscopy confirmed the presence of peptides on the surface of Fe3O4 NPs. Sequence analyses revealed that the probable binding mechanism between the peptide and Fe3O4 NPs might be driven by Pearson hard acid-hard base specific interaction and hydrogen bonds, accompanied with hydrophilic interactions and non-specific electrostatic attractions. The cell viability assay indicated a good cytocompatibility of peptide-bound Fe3O4 NPs. Furthermore, TVNFKLY peptide and an ovarian tumor cell A2780 specific binding peptide (QQTNWSL) were conjugated to afford a liner 14-mer peptide (QQTNWSLTVNFKLY). The binding and targeting studies showed that 14-mer peptide was able to retain both the strong binding ability to Fe3O4 NPs and the specific binding ability to A2780 cells. The results suggested that the Fe3O4-binding peptides would be of great potential in the functionalization of Fe3O4 NPs for the tumor-targeted drug delivery and magnetic hyperthermia. |
| File Format | HTM / HTML |
| ISSN | 09277765 |
| Journal | Colloids and Surfaces B: Biointerfaces |
| Volume Number | 141 |
| e-ISSN | 18734367 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-05-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Colloid and Surface Chemistry Medicine Physical and Theoretical Chemistry Surfaces and Interfaces Biotechnology |
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