Creative Biolabs provides custom construction service of high quality and diversity Hi-Affi™ phage display tendamistat library. Our scientists are enthused in offering our customers with the most appropriate project for each individual requirement.
Tendamistat, produced by Streptomyces tendae , is a 74 amino acids α-amylase inhibitor which can target a wide range of mammalian α-amylase to inhibit the hydrolysis of starch. It is a small size molecule with considerable stability, and the structural data is also available via high resolution NMR and X-ray analysis. The topology of tendamistat has shown very similar structure to an immunoglobulin domain, which may adopt multiple conformations. Tendamistat forms a β-sheet sandwich with six antiparallel β-strands arranged as two β-sheets, which are held together with two disulfide bonds that link at the strands 1 & 2 and the strands 4 & 6. By analogy with the CDR loops of immunoglobulins, the loops of tendamistat indicate similar function and may also be modified by mutagenesis. These features, therefore, enable tendamistat to become a potential choice as scaffold protein.
In practice, tendamistat has been employed as a kind of Ig-type scaffold to present conformationally constrained random peptides. In particular, the two loops of tendamistat, which comprising residues 38-40 and 60-65, seem to be permissive to randomization, and do not affect the α-amylase binding ability. Taking advantage of these, a tendamistat scaffold library was constructed and the scaffolds were tested for binding to A8 antibody which can recognize endothelin. The isolated tendamistat scaffolds still maintain the original inhibiting ability and are capable to specifically bind this target antibody. As a robust nature inhibitor, tendamistat is certainly attractive as protein scaffold, which different patterns could be recognized and detected the constructed tendamistat scaffold libraries. It also suggests that this scaffold can play a significant role in novel binding molecules selection.
Creative Biolabs has engineered upon phage display technology to develop a proprietary Hi-Affi™ phage display platform for the scaffold libraries construction. Comparing with the traditional phage display method, which fuse targets of interest to bacteriophage coat proteins and thereby displayed on the phage surface for selecting specific binders, Hi-Affi™ platform has integrated the trimer codon technology and NNK method which can achieve expanded diversity for the selection of high affinity target binders. By deploying this platform, our scientists can provide the clients with 100% precise mutant library construction with over 1010 diversity.
According to years of experience in scaffold library construction, Creative Biolabs own an elite team of experts to execute our standardized experimental process and professional information analysis. It is our commitment and guarantees to offer our global customers with the highest efficiency and quality technical service for their research and project development.
Fig. 1 Crystal structure of tendamistat. (PDB ID: 1OK0)