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LN1 peptide (C-TGTPARQ-C), is a 9-amino-acid cyclic peptide, featuring cysteine residues at both ends for disulfide bridge formation, is derived from innovative research published in ACS Applied Materials & Interfaces (DOI: 10.1021/acsami.3c07248). LN1 is meticulously engineered to target specific biological processes, making it an indispensable asset for scientists exploring cell adhesion, surface functionalization, and therapeutic development.
Applications in Research
The LN1 peptide (C-TGTPARQ-C) is optimized for a variety of high-impact research applications:
- Tissue Engineering: LN1 promotes cell adhesion and proliferation, making it ideal for designing bioactive scaffolds and hydrogels that mimic the extracellular matrix (ECM) for regenerative medicine.
- Biomaterial Functionalization: Use this peptide to modify surfaces of implants or nanoparticles, enhancing biocompatibility and targeting specific cellular receptors.
- Cell Signaling Studies: Investigate how LN1 modulates integrin-mediated signaling pathways, critical for understanding cell migration, differentiation, and survival.
- Drug Delivery Systems: Leverage its specific binding properties to develop targeted drug carriers, improving therapeutic efficacy in precision medicine.
- Wound Healing Research: Explore its role in accelerating tissue repair by facilitating interactions between cells and engineered matrices.
Functions and Mechanisms
The LN1 peptide (C-TGTPARQ-C) offers unique functional attributes rooted in its cyclic structure and sequence:
- Cell Adhesion Enhancement: The TGTPARQ core, flanked by cysteines forming a disulfide bond, binds integrins or ECM components, promoting robust cell attachment and spreading.
- Structural Stability: The cyclic nature, stabilized by the C-C disulfide bridge, ensures resistance to degradation and maintains bioactivity under physiological conditions.
- Selective Binding: Its arginine (R) and glutamine (Q) residues contribute to high-affinity interactions with target proteins, enabling precise molecular recognition.
Biological Importance
Highlighted in ACS Applied Materials & Interfaces, the LN1 peptide (C-TGTPARQ-C) is a key player in biomaterial-cell interactions:
- Regenerative Medicine: LN1’s ability to enhance cell-matrix adhesion supports the development of next-generation tissue scaffolds, vital for repairing damaged organs or tissues.
- Cancer Research: Its integrin-binding properties offer insights into tumor cell behavior, aiding studies on metastasis and tumor microenvironment engineering.
- Synthetic Biology: LN1 serves as a model peptide for designing bioinspired materials that replicate natural cellular environments, bridging biology and materials science.
Related sequences: LN2 (C-KNSMFAT-C) and LN3 (C-TNKHSPK-C)
Complement your research with our related peptides:
- LN2 Peptide (C-KNSMFAT-C): Enhance your studies with LN2, designed for applications in protein-surface interactions and antimicrobial coatings. Its methionine (M) and phenylalanine (F) residues offer unique hydrophobic and aromatic properties, perfect for cross-disciplinary biomaterial research.
- LN3 Peptide (C-TNKHSPK-C): Expand your toolkit with LN3, tailored for cell signaling and enzyme interaction studies. Featuring histidine (H) and lysine (K), it excels in pH-responsive systems and bioactive surface design.
Why Choose Our LN1 Peptide (C-TGTPARQ-C)?
- Ultra-High Purity: Synthesized at >98% purity, verified by HPLC and mass spectrometry for reliable, reproducible results.
- Flexible Formats: Available as lyophilized powder or custom solutions, with scalable quantities to meet your experimental needs.
- Research-Backed: Validated by peer-reviewed studies in ACS Applied Materials & Interfaces, ensuring relevance to cutting-edge science.
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