Fmoc-(R)-3-Amino-4-(2-thienyl)-butyric acid
98%
- Product Code: 104969
CAS:
269726-90-1
| Molecular Weight: | 407.48 g./mol | Molecular Formula: | C₂₃H₂₁NO₄S |
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| Density: | Storage Condition: | 2-8°C |
Product Description:
This compound is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS). It serves as a building block for introducing specific amino acid sequences into peptides. The Fmoc group acts as a protective group for the amine functionality, ensuring selective reactivity during the coupling process. The thienyl side chain in the structure provides unique properties, such as influencing peptide conformation and enhancing interactions with biological targets. This makes it valuable in the development of peptide-based drugs, especially those targeting enzymes, receptors, or other biomolecules. Its application is also seen in research for designing peptides with improved stability, bioavailability, and therapeutic efficacy. Additionally, it is utilized in the study of structure-activity relationships (SAR) to optimize peptide performance in various biological systems.
Sizes / Availability / Pricing:
| Size (g) | Availability | Price | Quantity |
|---|---|---|---|
| 0.100 | 10-20 days | ฿4,302.00 |
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| 0.250 | 10-20 days | ฿7,470.00 |
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| 1.000 | 10-20 days | ฿15,390.00 |
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Fmoc-(R)-3-Amino-4-(2-thienyl)-butyric acid
This compound is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS). It serves as a building block for introducing specific amino acid sequences into peptides. The Fmoc group acts as a protective group for the amine functionality, ensuring selective reactivity during the coupling process. The thienyl side chain in the structure provides unique properties, such as influencing peptide conformation and enhancing interactions with biological targets. This makes it valuable in the development of peptide-based drugs, especially those targeting enzymes, receptors, or other biomolecules. Its application is also seen in research for designing peptides with improved stability, bioavailability, and therapeutic efficacy. Additionally, it is utilized in the study of structure-activity relationships (SAR) to optimize peptide performance in various biological systems.
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