Immunoglobulin-Like β-Sandwich Protein Design

Through our comprehensive early discovery, nonclinical and commercialization services, Creative Biolabs is capable of providing our clients with a variety of customized services in protein engineering services for creating and screening a handful of proteins to meet the requirement of our worldwide customers. We are dedicated to reducing protein development time and promoting the therapeutic proteins to clinical trials for a wide range of disease treatment.

Introduction to Immunoglobulin-Like β-Sandwich Proteins

Immunoglobulin-like (Ig-like) β-sandwich protein is one of the most important structural motifs in proteins that plays a significant role in analyzing the function of conserved residues in proteins. Pilot studies have demonstrated that a wide variety of Ig-like domains have been identified in diverse proteins, such as cell receptors, muscle proteins, and immune cells. Meanwhile, previous studies have indicated that all Ig-like domains consist of two antiparallel β-sheets. Furthermore, Ig-like domains have been widely used in assessing the misfolding tendency and folding stability of a protein. Additionally, the folding mechanism of Ig-like domains has been also revealed in the past few years. Much data suggests that they share a similar folding pathway in protein families owing to the conserved folding nucleus. Therefore, the folding mechanism of Ig-like β-sandwich proteins has been predicted by comparing different Ig domains and fibronectin type III (fnIII) domains. Ig-like β-sandwich proteins have been designed to perform many biological functions and stable conformation.

The Immunoglobulin-Like β-Sandwich Protein Design. Fig.1 The Immunoglobulin-Like β-Sandwich Protein Design.


Natural proteins often need to be engineered before being used in the drug process of drug discovery and production. The mechanical stability in the Ig-like domain has been considered as a key element for a series of protein design and engineering. A wide collection of technologies has been developed for detecting the protein folding and their properties in designing different kinds of Ig-like β-sandwich proteins. Currently, Creative Biolabs offers a diverse range of synthetic binding protein engineering services to altering the structure and function of proteins in drug therapies. In a recent study, we have developed a panel of assays, including atomic force microscopy (AFM), X-ray crystallography, and recombinant DNA technology, to measuring folding properties in protein design and engineering. For example, AFM has been used to identify the determinants of mechanical stability in Ig-like domains from human cardiac titin at the molecule level.

Using the atomic force microscope to measure the molecular elasticity of single proteins. Fig.2 Using the atomic force microscope to measure the molecular elasticity of single proteins. (Carrion-Vazquez, 2000)

Creative Biolabs is a leader in the field of protein design and engineering for years. We will work with you to develop the most appropriate strategy that will offer the most meaningful data for your research. We utilize unrivaled, proprietary protein design, study data, product candidate, advanced project life-cycle management, as well as real-time data to ensure the ideal outcomes. If you are interested in our services, please contact us for more details. Let us know what you need and we will accommodate you. We look forward to working with you in the future.


  1. Carrion-Vazquez, M.; et al. Mechanical design of proteins studied by single-molecule force spectroscopy and protein engineering. Prog Biophys Mol Biol. 2000, 74(1-2): 63-91.

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