Vinculin (10-19)

Vinculin (10-19) is a synthetic peptide fragment derived from the N-terminal region of the cytoskeletal protein vinculin, a key component involved in cell adhesion, mechanotransduction, and the regulation of cytoskeletal dynamics. As a peptide corresponding to amino acids 10 through 19 of the full-length vinculin sequence, it serves as a valuable molecular tool for dissecting protein-protein interactions, mapping functional domains, and elucidating the biological roles of vinculin in cellular processes. Its defined sequence and biochemical properties make it particularly relevant for research focused on actin-binding proteins, focal adhesion complexes, and the modulation of cell-matrix interactions.

Protein-protein interaction studies: The 10-19 peptide fragment of vinculin is widely employed in research investigating the specific binding motifs responsible for vinculin's association with various cytoskeletal or adhesion partners. By serving as a competitive inhibitor or a molecular probe in binding assays, this peptide enables researchers to pinpoint the critical residues mediating vinculin's interaction with actin, talin, or other focal adhesion proteins. Such studies are instrumental in clarifying the mechanistic basis of cytoskeletal organization and the dynamic assembly of adhesion complexes.

Peptide mapping and epitope characterization: As a defined sequence from the vinculin N-terminus, this peptide is frequently utilized in epitope mapping experiments to identify antibody binding sites or to generate sequence-specific antibodies. By employing the peptide in immunoassays or as an immunogen, investigators can characterize the antigenic determinants of vinculin, facilitating the development of highly specific detection reagents for immunoblotting, immunofluorescence, or immunoprecipitation applications.

Cell signaling pathway analysis: The synthetic vinculin (10-19) peptide can be applied to studies focused on the regulation of cell adhesion signaling pathways. By introducing the peptide into cultured cells or in vitro systems, researchers can probe its effects on focal adhesion assembly, integrin-mediated signaling cascades, or actin cytoskeleton remodeling. These experimental approaches help elucidate how discrete vinculin domains contribute to downstream signaling events and the coordination of cellular responses to mechanical stimuli.

Peptide-based screening and inhibitor development: The defined sequence and structural properties of this peptide make it suitable for use in high-throughput screening platforms aimed at identifying modulators of vinculin-mediated interactions. By serving as a template or reference ligand, it supports the discovery and optimization of small molecules or biologics that selectively disrupt or enhance vinculin's functional interfaces. Such applications are particularly relevant in the context of drug discovery efforts targeting cell adhesion and migration processes.

Structural and conformational studies: In biophysical research, the vinculin (10-19) peptide is valuable for probing the structural determinants of protein-peptide interactions. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism, or X-ray crystallography can utilize this peptide to investigate the conformational flexibility, secondary structure propensity, or binding-induced folding events associated with vinculin's N-terminal region. These insights advance the understanding of how short linear motifs contribute to the dynamic regulation of larger protein assemblies within the cytoskeleton.

1. Sex differences in oxidative stress level and antioxidative enzymes expression and activity in obese pre-diabetic elderly rats treated with metformin or liraglutide

2. P-selectin and Complement’s Role in a Neonatal Model of Germinal Matrix Hemorrhage-Induced Secondary Injury

3. Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef

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

5. Characterization of Novel P-Selectin Targeted Complement Inhibitors in Murine Models of Hindlimb Injury and Transplantation