High Quality Fmoc-lys(dde)-Oh with the CAS number 150629-67-7 is a significant chemical product. The Fmoc group (9-fluorenylmethyloxycarbonyl) is a widely - used protecting group in peptide synthesis, and the lysine derivative with the Dde (1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl) group on the side - chain of lysine provides specific protection and reactivity. The product offers high quality and comes at the best price, which makes it an attractive choice for research laboratories and chemical synthesis companies.
Some of its basic parameters include a specific molecular structure that combines the Fmoc protective group on the amino - terminal and the Dde group on the lysine side - chain. This structure gives it unique chemical properties, such as stability under certain reaction conditions and the ability to be selectively deprotected under specific reagents or reaction environments.
This product is mainly used in the field of peptide synthesis. In peptide chemistry, protecting groups play a crucial role in controlling the reaction sites and ensuring the correct sequence of amino acids during the synthesis process. The Fmoc group can be easily removed under mild basic conditions, which allows for step - by - step peptide chain elongation. The Dde group on the lysine side - chain can be selectively removed in the presence of hydrazine, enabling further modification or connection at the lysine residue.
It is also used in the synthesis of complex peptides with multiple functional groups. Scientists can use this product to synthesize peptides with specific biological activities, such as antimicrobial peptides, peptide hormones, and peptide - based drugs. Additionally, it can be used in the study of protein - protein interactions, as synthetic peptides can mimic certain regions of proteins and be used as probes to understand the binding mechanisms.
When using High Quality Fmoc-lys(dde)-Oh in peptide synthesis, the first step is usually the coupling reaction. The Fmoc - protected amino acid is coupled to the growing peptide chain using appropriate coupling reagents, such as HBTU (O - (benzotriazol - 1 - yl) - N,N,N',N' - tetramethyluronium hexafluorophosphate) or DIC (N,N' - diisopropylcarbodiimide) in the presence of a base like DIPEA (N,N - diisopropylethylamine).
After the coupling reaction, the Fmoc group can be removed by treating the peptide with a mild base, such as 20% piperidine in DMF (N,N - dimethylformamide). The Dde group on the lysine side - chain remains intact during this process. When the specific modification at the lysine residue is required, the Dde group can be selectively removed by treatment with a solution of hydrazine in an appropriate solvent. After deprotection, further reactions can be carried out at the lysine residue, such as acylation or conjugation with other molecules.
Case 1: Synthesis of an Antimicrobial Peptide
In a research project focused on developing new antimicrobial peptides, scientists used High Quality Fmoc-lys(dde)-Oh. They first designed a peptide sequence with multiple lysine residues. By using the Dde - protected lysine, they could selectively modify these lysine residues after the main peptide chain was synthesized. After the Fmoc - based solid - phase peptide synthesis was completed, they removed the Dde groups at specific lysine positions and conjugated fatty acid chains to these lysine residues. This modification significantly enhanced the antimicrobial activity of the peptide, demonstrating the importance of using this product in the synthesis of functional peptides.
Case 2: Protein - Protein Interaction Study
In another study, researchers aimed to understand the binding mechanism between two proteins. They synthesized a peptide fragment using High Quality F
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