Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation.

ABSTRACT: Binding affinity and specificity are crucial factors that influence nanostructure control by biomineralization peptides. In this paper, we analysed the role that the oligomeric state of a silver biomineralization peptide plays in regulating the morphology of silver nanostructure formation. Oligomerization was achieved by conjugating the silver specific TBP biomineralization peptide to the p53 tetramerization domain peptide (p53Tet). Interestingly, the TBP-p53Tet tetrameric peptide acted as a growth catalyst, controlling silver crystal growth, which resulted in the formation of hexagonal silver nanoplates without consuming the peptide. The TBP-p53Tet peptide caps the surface of the silver crystals, which enhances crystal growth on specific faces and thereby regulates silver nanostructure fo

SUBMITTER: Sakaguchi T 

PROVIDER: S-EPMC5431226 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature