Peptide-Modified Dendrimers as Templates for the Production of Highly Reactive Catalytic Nanomaterials

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• 作者：Nicholas M. Bedford ; Rohit Bhandari ; Joseph M. Slocik ; Soenke Seifert ; Rajesh R. Naik ; Marc R. Knecht
• 刊名：Chemistry of Materials
• 出版年：2014
• 出版时间：July 22, 2014
• 年：2014
• 卷：26
• 期：14
• 页码：4082-4091
• 全文大小：559K
• ISSN：1520-5002

文摘

Peptide-driven nanomaterials synthesis and assembly has become a significant research thrust due to the capability to generate a range of multifunctional materials with high spatial precision and tunable properties. Despite the extensive amount of available literature, the majority of studies report the use of free peptides to drive synthesis and assembly. Such strategies are not an entirely accurate representation of nature, as many materials binding peptides found in biological systems are sterically constrained to a larger biological motif. Herein we report the synthesis of catalytic Pd nanomaterials using constrained peptides covalently attached to the surface of small, water-soluble dendrimers. Using the R5 peptide conjugated to polyamidoamine dendrimer as a bioconjugate, Pd nanomaterials were generated that displayed altered morphologies compared to nanomaterials templated with free R5. It was discovered that the peptide surface density on the dendrimer affected the resulting nanoscale morphology. Furthermore, the catalytic activities of Pd materials templated with R5/dendrimer are higher as compared to the R5-templated Pd materials for the hydrogenation of allyl alcohol, with an average increase in turnover frequency of 1500 mol product (mol Pd 脳 h)^鈭?. Small angle X-ray scattering analysis and dynamic light scattering indicate that Pd derived from R5/dendrimer templates remained less aggregated in solution and displayed more available reactive Pd surface area. Such morphological changes in solution are attributed to the constrained peptide binding motifs, which altered the Pd morphology and subsequent properties. Moreover, the results of this study suggest that constrained materials binding peptide systems can be employed as a means to alter morphology and improve resulting properties.