Coiled-coil domain-containing protein 110 (499-508)

Coiled-coil domain-containing protein 110 (499-508) is a synthetic peptide fragment derived from the larger coiled-coil domain-containing protein 110 (CCDC110), a protein implicated in various cellular processes involving cytoskeletal organization and intracellular signaling. The 499-508 amino acid region represents a specific segment within the protein's coiled-coil motif, a structural element known for mediating protein-protein interactions and contributing to the assembly of multiprotein complexes. By isolating this defined sequence, researchers gain a valuable biochemical tool for dissecting the functional properties and interaction networks of coiled-coil domains in cellular systems. The availability of such targeted peptide fragments is essential for advancing mechanistic studies and supporting a range of experimental approaches in protein science, cell biology, and structural biochemistry.

Peptide interaction studies: The 499-508 segment of CCDC110 is particularly suited for probing protein-protein interactions mediated by coiled-coil motifs. Utilizing this peptide in binding assays, pull-down experiments, or surface plasmon resonance analyses enables researchers to identify and characterize interaction partners that specifically recognize or bind to this portion of the parent protein. These studies can yield insights into the molecular determinants of coiled-coil recognition, the specificity of intermolecular contacts, and the assembly dynamics of protein complexes in which CCDC110 participates.

Structural biology research: As a well-defined peptide representing a functionally relevant region of a coiled-coil domain, the 499-508 fragment serves as an excellent model system for structural investigations. It can be employed in circular dichroism spectroscopy, nuclear magnetic resonance (NMR) studies, or crystallographic experiments to elucidate secondary structure, conformational stability, and folding behavior. Such analyses help clarify how short coiled-coil segments contribute to the overall architecture and mechanical properties of larger protein assemblies, informing the design of synthetic analogs or engineered protein scaffolds.

Antibody generation and epitope mapping: The synthetic peptide corresponding to residues 499-508 of CCDC110 provides a reliable antigen for the production of sequence-specific polyclonal or monoclonal antibodies. These antibodies are valuable for detecting the native protein in immunoassays, Western blotting, or immunofluorescence applications, as well as for mapping the accessibility and immunogenicity of the coiled-coil region within the full-length protein. Such reagents facilitate both basic research and the development of analytical tools for monitoring CCDC110 expression and localization in diverse biological samples.

Peptide-based functional assays: Incorporation of the 499-508 peptide into in vitro functional assays allows for direct testing of its biological activity or regulatory effects on cellular processes. For example, the peptide can be used to competitively inhibit endogenous coiled-coil interactions, disrupt multiprotein complex formation, or modulate downstream signaling pathways. These experimental strategies are instrumental in delineating the mechanistic roles of specific coiled-coil segments and in validating potential sites for targeted modulation within the broader context of protein function.

Biochemical assay development: The defined sequence and physicochemical properties of the CCDC110 (499-508) peptide make it a useful standard or control in various biochemical assays. It can be employed to calibrate detection systems, optimize assay conditions, or validate analytical methodologies that target coiled-coil domains. By providing a reproducible and well-characterized reagent, the peptide supports the development and refinement of high-throughput screening platforms, quantitative binding assays, and other experimental workflows that depend on precise molecular recognition and interaction analysis.

1. Glucagonlike peptide 2 analogue teduglutide: stimulation of proliferation but reduction of differentiation in human Caco-2 intestinal epithelial cells

2. Extended exenatide administration enhances lipid metabolism and exacerbates pancreatic injury in mice on a high fat, high carbohydrate diet

3. Spatiotemporal delivery of nanoformulated liraglutide for cardiac regeneration after myocardial infarction

4. Novel Peptide-Based PD1 Immunomodulators Demonstrate Efficacy in Infectious Disease Vaccines and Therapeutics

5. Proinsulin C-peptide and insulin: Limited pattern similarities of interest in inter-peptide interactions but no C-peptide effect on insulin and IGF-1 receptor signaling