Creative Biolabs provides the zinc finger library construction service using our Hi-Affi™ phage display platform. This platform can achieve desired libraries with high affinity and diversity for screening and selecting of a broad range of target epitopes.
Zinc finger, as a miniprotein composed of 26 amino acids, was firstly identified in a transcription study via Xenopus laevis (African clawed frog) and characterized by the coordination of one or more zinc ions in order to stabilize the fold. These proteins are now found with various binding properties which can also bind to DNA, RNA, protein or lipid substrates. Zinc finger is a member of the DNA-binding motifs family, contains multiple finger-like protrusions that can recognize a diverse set of DNA strings in a sequence-specific manner. The binding ability of zinc finger is considered to involve the sequences of finger domains and their linkers, as well as their number and structure order.
Zinc finger scaffold has been used as a conformational framework for the selection-driven design of novel DNA binding protein. It is ubiquitous in the biological world and a variety of zinc fingers have been identified in different superfamilies with distinct sequence and structure, which shown considerable versatility in binding modes. In addition, zinc finger scaffold has relatively stable structure, which is rarely undergo conformational change upon binding to the target. The zinc finger scaffold libraries can be constructed through phage display technology by substitutions of five amino acids in the α-helical portion. Then the zinc finger scaffold with great specificity and affinity can be selected that carries various therapeutic and research capacities.
Creative Biolabs has developed the unique Hi-Affi™ phage display platform for the generation of scaffold protein libraries. Phage display technology has become a major approach in selecting highly specific scaffolds for therapeutics discovery. It is a kind of gene expression and affinity selection, with the fusion of the proposed target gene with the bacteriophage coat proteins and thereby displayed on the phage surface; then by affinity enrichment method to select the specific phage peptide or protein. In order to improve the diversity of the scaffold libraries, our proprietary Hi-Affi™ platform has integrated the trimer codon technology and NNK method, which make it more suitable for sorting and isolating the high affinity protein or peptide targets. Through this platform, our scientists can generate high quality scaffold libraries with 100% precise mutant and over 1010 diversity.
Creative Biolabs is a long-term expert in the field of scaffold library construction, and has successfully constructed more than 50 scaffold libraries, such as DARPin, knottins, monobody, affilin and so on. Our experienced scientists are confident in delivering our clients with satisfying libraries that meets all their required specifications.
Fig. 1 Three-dimensional solution structure of a single zinc finger DNA-binding domain. (PDB ID:1ZNF)