Unlock Peptide Synthesis Efficiency: The Role of Fmoc-Cys(StBu)-OH in Protecting Cysteine Residues
Discover the indispensable role of Fmoc-Cys(StBu)-OH in modern peptide synthesis. This essential Fmoc-protected amino acid derivative is key to efficiently protecting cysteine residues and achieving complex peptide structures. Learn how its unique properties contribute to successful disulfide bond formation and unlock new possibilities in your research.
Get a Quote & SampleProduct Core Value
Fmoc-Cys(StBu)-OH
As a leading supplier in China, we offer Fmoc-Cys(StBu)-OH, a critical Fmoc-protected amino acid derivative vital for solid-phase peptide synthesis (SPPS). It provides robust protection for the cysteine thiol side chain, ensuring stability throughout peptide chain elongation. This allows for precise control over peptide bond formation, making it indispensable for synthesizing peptides with disulfide bridges and complex architectures. We are dedicated to providing high-quality chemical building blocks to meet the diverse needs of researchers and manufacturers globally.
- Essential for Fmoc-based SPPS: Utilized as a key building block in solid-phase peptide synthesis, ensuring efficient incorporation of protected cysteine residues.
- Cysteine Thiol Side Chain Protection: Offers reliable protection for the cysteine thiol, preventing unwanted side reactions during peptide elongation.
- Facilitates Disulfide Bridge Formation: Crucial for synthesizing peptides containing disulfide bonds, which are vital for many bioactive peptides.
- Stable and Reliable: Exhibits excellent stability during standard SPPS conditions, including acid and base treatments, ensuring integrity throughout the synthesis process.
Advantages of Using Fmoc-Cys(StBu)-OH
Enhanced Peptide Purity
Leverage Fmoc-Cys(StBu)-OH to achieve superior peptide purity by minimizing side reactions that can occur with unprotected cysteine residues during solid-phase peptide synthesis.
Controlled Disulfide Bond Formation
The strategic protection offered by Fmoc-Cys(StBu)-OH is key to controlled disulfide bond formation, enabling the synthesis of peptides with specific structural configurations and enhanced biological activity.
Compatibility with SPPS Strategies
This Fmoc-protected amino acid derivative is highly compatible with established Fmoc/tBu SPPS strategies, allowing for seamless integration into existing peptide synthesis workflows.
Key Applications
Peptide Synthesis
A fundamental building block in the synthesis of peptides, including therapeutic peptides and research-grade peptides, for various biochemical and pharmaceutical applications.
Organic Synthesis
Serves as a versatile reagent in broader organic synthesis, particularly when introducing protected cysteine functionalities into complex molecules.
Biochemical Research
Essential for researchers studying protein structure, function, and the role of disulfide bonds in biological systems through the synthesis of specific peptide models.
Drug Discovery
Supports drug discovery efforts by enabling the synthesis of novel peptide-based therapeutics and diagnostics that rely on precise cysteine modifications.