Collagen-mimetic peptides (CMP) in their folded conformation form nanoparticle-like support for immobilization of organometallic catalysts. Having heterogeneous catalysts in one-pot we combine the advantage of defined active sites of peptides. We have shown that different catalysts can be placed in the well-defined spatial arrangement allowing for more than one transformation simultaneously. We tested this hypothesis by immobilizing two organometallic catalyst on a CMP: 4-carboxy-1,10-phenanthroline copper (II) complex and a phosphine-palladium (II) complex on a collagen peptide. The former was immobilized via lysine residue and the latter via arginine, 8.58 Å – 11.44 Å apart. This formed a pocket for our synthesized substrate to undergo both transformations. Results suggest dual catalysts can display enhanced activity, but exact control of reaction selectivity is difficult. Reaction conditions, including substrate design, must be optimized further to synthesize a desired product. Compatibility between dual catalysts must also always be considered.
|Commitee:||Shon, Young-Seok, Derakhshan, Shahab|
|School:||California State University, Long Beach|
|Department:||Chemistry and Biochemistry|
|School Location:||United States -- California|
|Source:||MAI 82/6(E), Masters Abstracts International|
|Subjects:||Biochemistry, Nanoscience, Organic chemistry|
|Keywords:||Collagen-mimetic peptides , Nanoparticles, Immobilization , Organometallic catalysts , Spatial arranagement, Reaction selectivity|
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