| Nature offers unique insights and solutions to complex problems encountered in materials synthesis as a result of highly developed biomineralization processes. Fundamentally, biological systems exhibit exquisite control and unique structural diversity in the biosynthesis of extended materials such as laminate composites, magnetic materials found in migratory birds, and various toxic metal clusters, through the use of templates. This is best exemplified by the detoxification of CdS nanoparticles via small phytochelatin peptides (gammaEC)nG and the selective mineralization of iron oxyhydroxide nanoparticles within the spatially defined cavity of the iron storage protein ferritin. By analogy, we have explored this biological control by using a diverse collection of biologically relevant ligands/templates to direct nanocluster formation. These include single amino acids, small synthetic peptide epitopes, helical peptides selected from a combinatorial library, biomimetic peptide dendrimers, engineered heat shock proteins, and gold reducing viruses. Consequently, these produced a matrix of nanoclusters with a broad scope of stability, reactivity, dispersity, crystallinity, morphology, self-assembly, and the ability to elicit an antibody response. Most notably, a histidine rich peptide epitope (HRE) from HRP II of Plasmodium falciparum successfully stabilized a set of nanoclusters and provided an antigenic peptide coat that was recognized by monoclonal antibodies to HRP II of malaria. The use of bioligands to design nanocluster-peptide interfaces provides numerous applications for biomaterials as diagnostic agents or the assembly of multi-component devices. |
