357271-55-7

Usage

Uses

Used in Peptide Synthesis:
Fmoc-β-HomoTrp(Boc)-OH is used as a protected amino acid for the synthesis of peptides. The Fmoc group protects the amine group of the β-HomoTrp residue, preventing unwanted side reactions during the assembly process. This ensures that the β-HomoTrp residue can be incorporated at a specific position within the peptide sequence with precision.
Used in Organic Chemistry:
In the field of organic chemistry, Fmoc-β-HomoTrp(Boc)-OH serves as an important intermediate for the synthesis of various organic molecules. The presence of the Fmoc and Boc protective groups allows for selective reactions and controlled synthesis pathways, enabling the creation of complex molecular structures with high yields and purity.
Used in Pharmaceutical Development:
Fmoc-β-HomoTrp(Boc)-OH is utilized in the development of pharmaceuticals, particularly for the creation of peptide-based drugs. Fmoc-β-HomoTrp(Boc)-OH's ability to be incorporated into peptides with specific structural requirements makes it a valuable tool in the design and synthesis of novel therapeutic agents with targeted biological activities.
Used in Research and Development:
In academic and industrial research settings, Fmoc-β-HomoTrp(Boc)-OH is employed for the exploration of new chemical reactions and the synthesis of innovative compounds. Its role as a protected amino acid allows researchers to investigate the properties and potential applications of peptides containing the β-HomoTrp residue, contributing to the advancement of scientific knowledge and the discovery of new materials and drugs.

Upstream product

• 143824-78-6 3-[(S)-2-carboxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)ethyl]indole-1-carboxylic acid tert-butyl ester 
• 357271-53-5 (S)-1-diazo-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-4-{N-[(tert-butoxy)carbonyl]indol-3-yl}butan-2-one 

Relevant academic research and scientific papers

Peptide folding induces high and selective affinity of a linear and small β-peptide to the human somatostatin receptor 4

β-Peptides with side chains in the 2- and 3-positions on neighboring residues (of (S) configuration) are known to fold and form a turn (similar to an α-peptidic β-turn). Thus, we have synthesized an appropriately substituted β-tetrapeptide derivative to mimic the hormone somatostatin in its binding to the human receptors hsst1-5, which is known to rest upon a turn containing the amino acid residues Thr, Lys, Trp, and Phe. The N-acetyl-peptide amide Acβ3-HThr-β2-HLys-β3 -HTrp-β3-HPhe-NH2 (1) indeed shows all characteristics of the targeted turnmimic: Lys CH2 groups are in the shielding cone of the Trp indole ring (by NMR analysis, Figure 2) and there is high and specific nanomolar affinity for hsst4 receptor (Table 1). In contrast, the isomer 2 bearing the Lys side chain in 3-, rather than in the 2-position, has a 1000-fold smaller affinity to hsst4. The syntheses of the required Fmoc-protected β-amino acids (8-11, 17) are described (Schemes 1-3). Coupling of the β-amino acids was achieved by the manual solid-phase technique, on Rink resin.