Creative BioMart is a well-known expert who uses various protein domains as non-antibody scaffolds to produce synthetic binding proteins that have the ability to bind to molecules. With years of experience, we successfully designed immunoglobulin-like β-sandwich binding protein based on non-antibody scaffolds to precisely meet customer requirements.

Introduction of Immunoglobulin-Like Domains

Immunoglobulin-like (Ig-like) β-sandwich is one of the most common structural motifs and plays an important role in analyzing the functions of conserved residues in proteins. Ig-like domains are widely found in proteins with multiple functions (extracellular matrix proteins, muscle proteins, immune system proteins, cell surface receptors and enzymes), including immunoglobulin, fibronectin type Ⅲ and cadherin super family. All the Ig-like proteins have two antiparallel β sheets packed against each other and a similar Greek key strand topology. Although they have very different amino acid sequences, they have similar folding pathways. The folding of different Ig-like β has a common feature-sandwich protein, there is a strong correlation between folding rate and stability. Ig-like domains have been widely used to assess the misfolding tendency and folding stability of proteins.

Fig 1. FlaF is a β-Sandwich protein that anchors the archaellum in the archaeal cell envelope by binding the S-Layer protein. (Banerjee A, et al., 2015)

Services

Natural proteins often need to be engineered before they can be used in the drug process of drug discovery and production. The folding properties of Ig-like domain proteins are considered to be key factors in protein design and engineering, and their number has increased significantly during the evolutionary process associated with the development of the adaptive immune system. Creative BioMart provides immunoglobulin-like β-sandwich protein services to change the structure and function of proteins in drug therapy. In addition, we also use advanced technology to identify the functions and characteristics of Ig-like domains, including their size, diversity of interactions, their binding strength, glycosylation, and their organization with other proteins. Our immunoglobulin-like β-sandwich protein can be used for disease treatment and mechanism discovery, and execution of many biological functions and stable conformations.

Creative BioMart has been continuously developing immunoglobulin-like β-sandwich domains, is committed to synthesizing application-type proteins and shortening the development time of proteins, and pushing therapeutic proteins into clinical trials for the treatment of a wide range of diseases. Based on the protein engineering platform, we have successfully designed a variety of platforms for different applications to produce special proteins. We will work with you to develop the most appropriate strategy and provide the most meaningful data for your research for accelerating the research of life sciences. If you are interested in our services, please do not hesitate to contact us for more information.

Reference

1. Banerjee A, Tsai CL, et al. (2015) FlaF Is a β-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein. Structure. 23(5): 863-872.

• Avimers Protein Design
• Repeat Protein Design
• Single Loop Protein Design
• Zinc Finger Protein Design
• α-Helical Scaffolds Protein Design
• β-Barrel Protein Design
• β-Sheet Surface Protein Design