期刊
ACS APPLIED MATERIALS & INTERFACES
卷 10, 期 22, 页码 18601-18609出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsami.8b05148
关键词
peptides; metal-organic frameworks; surface functionalization; phage display and drug delivery
资金
- Welch Foundation [F-1929, F-1904]
- National Science Foundation through the Center for Dynamics and Control of Materials: an NSF MRSEC [DMR-1720595]
We report a noncovalent surface functionalization technique for water-stable metal-organic frameworks using short peptide sequences identified via phage display. Specific frameworks-binding peptides were identified for crystalline Zn(MeIM)(2) (MeIM: 2-methylimidazole, ZIF-8), semiamorphous Fe-BTC (BTC: 1,3,5-benzene-tricarboxylate), and Al(OH)(C4H2O4) (MIL-53(Al)-FA, FA: fumaric acid), and their thermodynamic binding affinities and specificities were measured. Electron microscopy, powder X-ray diffraction, and gas adsorption analysis confirmed that the peptide-functionalized frameworks retained similar characteristics compared to their as-synthesized counterparts. Confocal laser-scanning microscopy demonstrated that peptide was localized on the surface of the frameworks, whereas surface area measurements showed no evidence of pore blockage. Finally, we measured the pH-dependent release of fluorescein from peptide-functionalized frameworks and discovered that peptide binding can attenuate fluorescein release by improving framework stability under low pH conditions. Our results demonstrate that phage display can be used as a general method to identify specific peptide sequences with strong binding affinity to water-stable metal-organic frameworks and that these peptides can alter drug release kinetics by affecting framework stability in aqueous environments.
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