Orthogonal Labeling of M13 Minor Capsid Proteins with DNA to Self-Assemble End-to-End Multiphage Structures

M13 bacteriophage has been used as a scaffold to organize :materials for various applications. Building more complex multiphage devices requires precise control of interactions between, the M13 capsid proteins. Toward we engineered a loop structure onto the pIII capsid protein of M13 bacteriophage to enable sortase-me labeling reactions for C-terminal display. Combining with N-terminal sortase-mediated labeling, we thusc created a phage scaffold that can he labeled orthogonally on three capsid proteins: the body and both ends. We show that covalent attachment of attachment different DNA ohgonucleotides at the ends of the new phage structure enables formation of multiphage particles oriented in a specific order. These have potential as nanascale scaffolds for multi-material devices.