273221-73-1

Usage

Uses

Used in Organic Synthesis:
N-Boc-3-iodo-DL-phenylalanine is used as a key intermediate for the preparation of complex organic molecules, leveraging its unique structure to facilitate the synthesis of a variety of compounds.
Used in Pharmaceutical Research:
In pharmaceutical research, N-Boc-3-iodo-DL-phenylalanine is utilized as a building block for the synthesis of pharmaceuticals and bioactive molecules, contributing to the development of new drugs and therapeutic agents.
Used in Peptide and Protein Therapeutics:
N-Boc-3-iodo-DL-phenylalanine is employed as an important intermediate in the preparation of peptide and protein therapeutics, playing a crucial role in the synthesis of biologically active peptides and proteins.
Used in Protein Structure and Function Studies:
N-Boc-3-iodo-DL-phenylalanine is also used as a tool in the study of protein structure and function, providing insights into the behavior and properties of proteins through its reactivity and structural characteristics.

Upstream product

• 856222-40-7 diethyl [(tert-butoxycarbonyl)amino](3-iodo-benzyl)malonate 
• 49617-83-6 m-Iodobenzyl bromide 
• 102831-44-7 diethyl tert-butoxycarbonylaminomalonate 

Downstream Products

• 273221-75-3 (S)-2-((tert-butoxycarbonyl)amino)-3-(3-iodophenyl)propanoic acid 
• 478183-66-3 Boc-3-iodo-D-phenylalanine 

Relevant academic research and scientific papers

Antibacterial macrocycles with substituted biphenyl

The invention relates to antibacterial macrocycles with substituted biphenyl and processes for their preparation, their use for the treatment and/or prophylaxis of diseases, and their use for the production of medicaments for the treatment and/or prophylaxis of diseases, especially of bacterial infections.

Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design

Cathepsin B is a member of the papain superfamily of cysteine proteases and has been implicated in the pathology of numerous diseases, including arthritis and cancer. As part of an effort to identify potent, reversible inhibitors of this protease, we examined a series of dipeptidyl nitriles, starting with the previously reported Cbz-Phe-NH-CH2CN (19, IC50 = 62 μM). High-resolution X-ray crystallographic data and molecular modeling were used to optimize the P1, P2, and P3 substituents of this template. Cathepsin B is unique in its class in that it contains a carboxylate recognition site in the S2′ pocket of the active site. Inhibitor potency and selectivity were enhanced by tethering a carboxylate functionality from the carbon α to the nitrile to interact with this region of the enzyme. This resulted in the identification of compound 10, a 7 nM inhibitor of cathepsin B, with excellent selectivity over other cysteine cathepsins.