Creative BioMart is a well-known expert who is committed to developing a variety of protein biomaterials as multifunctional platforms to study and solve various challenges in regenerative medicine. With years of experience, we provide customized services for calmodulin-based materials to precisely meet customer requirements.

Introduction of Calmodulin

Calmodulin (CaM) is a 16.5 kDa protein that regulates many Ca²⁺ sensitive pathways, including neuronal communication and muscle contraction, acting as a switch in the activation of many enzymes and proteins. CaM has a dumbbell-shaped structure with two folded domains connected by flexible linkers in solution. The calmodulin-binding domain of the target protein is contained in a 20-residue long amino acid sequence with no apparent amino acid sequence homology. In addition, CaM undergoes a conformational change upon binding of four Ca²⁺ ions that allows it to reversibly associate with CaM-binding domains present in over 100 different proteins. Based on these properties, the researchers used CaM as a sensory motif, leucine zipper as self-assembly motifs, random helical hydrophilic spacers confer flexibility and solubility, and various CaM-binding domains as actuator motifs. Calcium-modulated plasmonic switches were also fabricated using the unique capabilities of CaM as a biosensor.

Fig 1. Development and Characterization of Calmodulin-Based Copolymeric Hydrogels. (Fox C S, et al., 2020)

Services

Calmodulin motifs represent one of the more recent additions to the list of peptide domains included in a variety of protein-engineered materials. As a leading service provider of protein engineering, Creative BioMart uses new technologies in molecular sensing and signal transduction to create a large number of precise composition and materials of known Ca²⁺ sensitivity. The services we can provide include:

• Our scientists master a variety of NMR and spectroscopy experiments to help determine the CAM-binding structure of synthetic peptides containing various CAM-binding domains. Real-time changes in CaM dynamics, orientation, and structure with Ca²⁺ ion concentration can also be studied over long periods of time with the aid of high-resolution localized surface plasmon resonance spectroscopy.
• We designed a highly specific biosensor that exploits the ability of calmodulin to change conformation upon binding to peptide and protein ligands. This sensor can control the activity of the β-lactamase export domain and exhibits up to 120-fold higher catalytic activity. For the detection of toxins and other clinically relevant biomarkers.
• Based on the precise tunability of protein engineering, we can replace the CaM domain and the inactive N-terminal cutinase domain with any peptide drug or protein of interest, immobilize it on the surface and present an active site-directed ligand. For basic cell biology, tissue engineering and protein science research.

Creative BioMart is committed to developing calmodulin-based materials for global pharmaceuticals to manufacture innovative biosensor detection systems and develop therapeutic calmodulin scaffolds. 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. Vogel H J, Zhang M. (1995) Protein engineering and NMR studies of calmodulin[M]. Signal Transduction Mechanisms. Springer, Boston, MA, 3-15.
2. Fox C S, Berry H A, Pedigo S. (2020) Development and Characterization of Calmodulin-Based Copolymeric Hydrogels[J]. Biomacromolecules. 21(6): 2073-2086.

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