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 β-sheet surface binding protein based on non-antibody scaffolds to precisely meet customer requirements.

Introduction of β-Sheet Surface Protein

β-sheet is one of the main secondary structure features of proteins, consisting of extended polypeptide chains (beta-chains) connected by a network of hydrogen bonds. β-sheets usually have one side facing the protein core and another side facing the solvent, where the residues facing the solvent have a significant effect on the stability of the protein. β-sheet protein domains are ubiquitous in nature and have a wide range of functions: transportation of hydrophobic molecules, carbohydrate recognition and enzyme treatment, as well as viral capsids and antibody scaffolds. Under such circumstances, more and more researchers are devoted to understanding the structural and biological characteristics that contribute to the stability of β-sheet proteins. For example, tenascin (TNfn3) molecules are used to redesign β-sheet surface protein domains, or to increase the number of salt bridges (glutamic acid or aspartic acid paired with lysine or arginine) to optimize the interaction of β-sheet protein surface to improve stability. In addition, studies have shown that mutations in the β-sheet sequence are essential for regulating protein functions.

Fig 1. Design of amyloid b-sheet mimics. (Cheng P N, et al., 2012)

Services

β-sheet surface proteins have been widely used as attractive scaffolds for computational protein design. As a leading service provider of protein engineering, Creative BioMart can analyze the topological structure and interaction of β-sheet proteins for rapid modeling of 3D structures. At the same time, we consider a variety of energy factors (side chain rotamer preference, van der Waals force, static electricity and desolvation effects) to design β-sheet surface proteins. For example, we integrate TNfn3 molecules, salt bridges, and aromatic amino acids into β-sheet surface proteins to improve stability. In addition, we provide a series of new protein design services with curved β-sheet surfaces, which act as binding sites for other molecules and change protein functions. For example, we formed self-assembled oligopeptides based on β-sheet secondary structure: hydrogel culture materials.

Creative BioMart has established a mature β-sheet surface proteins design platform. These highly stable proteins provide new ways to treat the diseases they involve by controlling β-sheet interactions, from improved diagnostic tests and medical treatments to more effective chemical reaction catalysis in industrial processes. Our design of β-sheet surface protein has received a lot of recognition and praise from customers. The enzyme produced can reduce chemical waste and improve the efficiency of chemical reactions. It can also be used to detect food and environmental toxins.

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.

References

1. Kim DN, Jacobs TM, Kuhlman B. (2016) Boosting protein stability with the computational design of β-sheet surfaces. Protein Sci. 25(3): 702-710.
2. Marcos E, Basanta B, et al.. (2017) Principles for designing proteins with cavities formed by curved β sheets. Science. 355(6321): 201-206.
3. Cheng P N, Liu C, Zhao M, et al. (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity[J]. Nature chemistry. 4(11): 927-933.

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