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Creative Biolabs provides professional service for Min-23 library construction. With years of scaffold library construction experience, our scientists are able to generate high affinity Min-23 library by Hi-Affi™ phage display platform.
Min-23 is a five amino acids N-terminal truncated Ecballium elaterium trypsin inhibitor II (EETI-II), results in the stably folded 23-residue peptide, which devoid of an active site, and consists of only two disulfide bridges instead of three found in the parent protein. It is recognized as one of the shortest peptides containing a cystine-stabilized β-sheets (CSB) motif enclosing a stable autonomous folding unit and contribute to a high Tm of 100 °C. The autonomous folding unit is formed by a small triple-stranded β-sheet and allows it to fold in a near native manner.
Because of the features like small size, high stability, easy synthesis and no naturally occurring active site, Min-23 is a suitable scaffold for developing new bioactive molecules. Relevant researches have demonstrated the feasibility that the core CSB motif in Min-23 is permissive for a series of modification, such as grafting recognition sites or active sites to the scaffold and inducing variant sites through mutation technology. It is accessible to proceed 8 or 10 amino acids substitutions within a single exposed β-turn on the surface of Min-23 scaffold. In addition, it is also available to randomize sequences on a β-turn of Min-23 and generate phage display libraries to against different target molecules for discovering novel biological specificities. For instance, Souriau et al. (2005) confirmed the ability of loop insertion for Min-23 by using peptide epitopes from hemagglutinin (HA) and Gla-protein (E) and isolated 21 new specific binders against 7 different targets from a Min-23 library. Therefore, as a novel scaffold, Min-23 is possible to provide a wide range of applications in various biological and pharmaceutical areas.
Creative Biolabs own a proprietary Hi-Affi™ phage display platform for our scaffold libraries construction. This technology is based on the phage display technology, which is a method for displaying target of interest on the surface of bacteriophage coat proteins, combined with trimer codon technology and NNK methods. This advanced platform is more suitable for sorting and isolating the high affinity protein or peptide targets, which enable Creative Biolabs to offer 100% precise mutant library construction with over 1010 diversity.
Creative Biolabs has long-term extensive experience in the field of scaffold library construction. Our scientists are pleased to provide the best service to promote customers’ research and project with high efficiency and competitive price.
Fig. 1 Schematic representation of Min-23 (Souriau et al. 2005)
Souriau, C., Chiche, L., Irving, R. and Hudson, P. (2005) New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold, Biochemistry, 44(19), 7143-7155.
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