Coiled-coil domain-containing protein 110 (196-204)

Coiled-coil domain-containing protein 110 (196-204) is a synthetic peptide fragment derived from the sequence of the human coiled-coil domain-containing protein 110 (CCDC110), specifically encompassing amino acids 196 to 204. This peptide represents a section of the protein's coiled-coil motif, a structural element known for mediating protein-protein interactions, oligomerization, and scaffolding functions in a variety of cellular processes. The unique sequence and structural characteristics of this peptide make it a valuable tool for researchers investigating the molecular mechanisms of coiled-coil domains, protein assembly, and cellular architecture. Its defined region within CCDC110 provides a focused approach for studying the biological relevance of this domain in cellular and molecular research contexts.

Protein-protein interaction studies: The 196-204 peptide fragment of CCDC110 is frequently utilized in in vitro assays designed to elucidate the mechanisms of coiled-coil mediated protein-protein interactions. By serving as a model substrate or binding motif, it enables the detailed characterization of interaction partners and the mapping of binding interfaces within larger protein complexes. This application is particularly relevant in the context of cytoskeletal organization and nuclear structure, where coiled-coil domains play a pivotal role in maintaining cellular integrity.

Structural biology research: As a representative segment of a coiled-coil motif, this peptide supports the structural analysis of protein folding and assembly. It can be incorporated into biophysical studies employing techniques such as circular dichroism spectroscopy, X-ray crystallography, or nuclear magnetic resonance (NMR) spectroscopy to investigate the conformational stability, helical propensity, and oligomerization behavior of coiled-coil sequences. These insights are critical for understanding the fundamental properties that govern the formation and stability of coiled-coil structures in larger proteins.

Peptide-based inhibitor design: The defined sequence of the CCDC110 (196-204) fragment provides a template for the rational design of peptide-based inhibitors or mimetics targeting coiled-coil interactions. Researchers can use the peptide as a scaffold to develop analogs or modified sequences that competitively disrupt specific protein-protein interactions involving coiled-coil motifs. Such strategies are instrumental in probing the functional significance of these domains in cellular signaling, scaffolding, or structural assembly.

Antibody generation and epitope mapping: The synthetic peptide is well-suited for use as an immunogen in the production of sequence-specific antibodies against the CCDC110 protein or for fine mapping of antibody epitopes. By presenting a defined and accessible region of the protein, it facilitates the development of reagents for immunodetection, localization studies, or immunoprecipitation assays, thereby supporting the broader investigation of CCDC110's cellular functions and distribution.

Assay development and validation: The CCDC110 (196-204) peptide serves as a valuable standard or positive control in the development and optimization of peptide-based assays, including enzyme-linked immunosorbent assays (ELISA), surface plasmon resonance (SPR) analyses, or mass spectrometry workflows. Its well-characterized sequence and defined biochemical properties enable reliable assay calibration, sensitivity testing, and validation of detection reagents, enhancing the reproducibility and robustness of experimental protocols in coiled-coil protein research.

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