CLPTRHMAC (disulfide bond: 1-9)

What is CLPTRHMAC (disulfide bond: 1-9)

**Introduction to CLPTRHMAC (Disulfide Bond: 1-9)** CLPTRHMAC is a synthetic peptide featuring a critical disulfide bond between cysteine residues at positions 1 and 9, stabilizing its tertiary structure and enhancing biological activity. This cyclic peptide is designed for applications in drug development, biochemical research, and targeted therapeutics, leveraging its constrained conformation for improved binding affinity and specificity. The disulfide linkage ensures structural integrity, making it resistant to enzymatic degradation and suitable for in vitro and in vivo studies. CLPTRHMAC holds potential in modulating protein-protein interactions, enzyme inhibition, or receptor targeting, offering a versatile tool for advancing peptide-based therapeutics. Its well-defined structure and stability make it a promising candidate for innovative biomedical applications. (Word count: 100)

Preparation Process: To prepare CLPTRHMAC (disulfide bond: 1-9), follow these steps: 1. **Solid-Phase Peptide Synthesis (SPPS)**: Use Fmoc chemistry to assemble the linear peptide sequence on a resin. 2. **Selective Deprotection**: Remove protecting groups (e.g., Trt for Cys1 and Cys9) while keeping other side chains protected. 3. **Disulfide Formation**: Oxidize the free thiols of Cys1 and Cys9 using air or a mild oxidant (e.g., DMSO, I₂) in a diluted solution to form the 1-9 disulfide bond. 4. **Cleavage and Deprotection**: Treat the resin with TFA to cleave the peptide and remove remaining protecting groups. 5. **Purification**: Isolate the product via HPLC and confirm by mass spectrometry.

Usage Scenarios: CLPTRHMAC (disulfide bond: 1-9) is a cyclic peptide with a disulfide bridge between cysteine residues at positions 1 and 9, enhancing structural stability. It is primarily used in biochemical research to study peptide-protein interactions, receptor binding, and molecular recognition due to its constrained conformation. The compound serves as a model for investigating disulfide bond formation and its role in peptide folding and bioactivity. In drug discovery, CLPTRHMAC is explored for its potential as a scaffold for designing bioactive peptides with improved stability and specificity. Additionally, it aids in developing enzyme inhibitors, antimicrobial agents, and targeted therapeutics by mimicking natural peptide motifs.

CLPTRHMAC (disulfide bond: 1-9) Basic Info

CLPTRHMAC (disulfide bond: 1-9) Price