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 α-Helical binding protein based on non-antibody scaffolds to precisely meet customer requirements.

Introduction of α-Helical Protein

Alpha helix is the main element of secondary structure involved in structural folding and stability, and may also participate in function by binding to receptor molecules. An α-helix has 3.6 residues per turn, meaning amino acid side chains that are three or four residues apart are bought together in space and so α-helices are stabilized by hydrogen bond formation between the carbonyl oxygen of one amino acid, and the amide proton of another amino acid four residues further along the peptide chain. It is important to note that alpha helices have an essential role in the stability of larger protein structures. Studies have shown that the breaking of the alpha helix in a protein can lead to local unwinding and loss of function. Alpha helices are also important in the binding of DNA. Studying the failure of alpha helices can help understand malfunctions in certain biological systems.

Fig 1. α-Helical Protein Assembly Motifs. (Kohn WD, et al., 1997)

Services

α‐Helices were extracted from the Protein Data Bank (PDB), some amino acids had differential propensity values for adopting helical conformation in short, medium and long α‐Helices. As a leading service provider of protein engineering, Creative BioMart can detect alpha helices in proteins through a variety of spectroscopic techniques without the need to determine their three-dimensional structure. In addition, we can perform detailed neighborhood related sequence analysis on the α-helix in the protein, and design an α-helix scaffold protein with maximum conformational stability under specific conditions.

In protein structure, helix is an important shape and sequence selective recognition motif for the interaction between protein and protein nucleic acid. Based on the strategy of stabilizing short peptides in a-helical conformation, Creative BioMart has successfully established an α-helices scaffold platform. Our scientists rely on two paths: searching for new folds in the structure space and searching for the sequences that lead to the new folds in the sequence space to find new protein folds. A major breakthrough has been made. For example, the α-helical mimics we designed provide promising lead compounds for biological applications. The successful and rational design and engineering of transmembrane α-helical barrel proteins have had a significant impact on bio-nanotechnology and synthetic biology.

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. Garner J, Harding MM. (2007) Design and synthesis of alpha-helical peptides and mimetics. Org Biomol Chem. 5(22): 3577-3585.
2. Wang J, Feng JA. (2003) Exploring the sequence patterns in the alpha-helices of proteins. Protein Eng. 16(11): 799-807.
3. Kohn WD, Mant CT, Hodges RS. (1997) Alpha-helical protein assembly motifs. J Biol Chem. 272(5): 2583-2586.

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