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Peptide-Mediated Synthesis of Zeolitic Imidazolate Framework-8: Effect of Molecular Hydrophobicity, Charge Number and Charge Location
Three amphiphilic peptides with varied molecular hydrophobicity, charge number and charge location have been designed as regulators to modulate the crystal growth of zeolitic imidazolate framework-8 (ZIF-8). All three peptides can interact with ZIF-8 to inhibit {100} facet growth and produce truncat...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538180/ https://www.ncbi.nlm.nih.gov/pubmed/34685115 http://dx.doi.org/10.3390/nano11102665 |
Sumario: | Three amphiphilic peptides with varied molecular hydrophobicity, charge number and charge location have been designed as regulators to modulate the crystal growth of zeolitic imidazolate framework-8 (ZIF-8). All three peptides can interact with ZIF-8 to inhibit {100} facet growth and produce truncated cubic crystals. The peptide’s molecular hydrophobicity plays a dominant role in defining the final morphology and size of the ZIF-8 crystals. The peptides with less charge and higher hydrophobicity can promote nuclei formation and crystal growth to give smaller ZIF-8 crystals. However, the charge located in the center of the molecular hydrophobic region has little effect on the crystal nucleation and growth due to the shielding of its charge by molecular aggregation. The study provides insights into the effect of molecular charge and hydrophobicity on ZIF-8 crystal growth and is helpful for guiding the molecular design for regulating the synthesis of metal-organic framework materials. |
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