366780-92-9

Basic information

• Product Name: N_α-carbobenzyloxy-L-2-amino-3-acryloylaminopropionic acid
• Synonyms: N_α-carbobenzyloxy-L-2-amino-3-acryloylaminopropionic acid
• CAS NO: 366780-92-9
• Molecular Weight: 292.291
• Mol File: 366780-92-9.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: N_α-carbobenzyloxy-L-2-amino-3-acryloylaminopropionic acid(CAS DataBase Reference)
• NIST Chemistry Reference: N_α-carbobenzyloxy-L-2-amino-3-acryloylaminopropionic acid(366780-92-9)
• EPA Substance Registry System: N_α-carbobenzyloxy-L-2-amino-3-acryloylaminopropionic acid(366780-92-9)

Safety Data

• Hazardous Substances Data: 366780-92-9(Hazardous Substances Data)

Upstream product

• 2304-96-3 N-benzyloxycarbonyl-L-asparagine 
• 35761-26-3 (S)-3-amino-2-(((benzyloxy)carbonyl)amino)propanoic acid 
• 814-68-6 acryloyl chloride 

Downstream Products

• 366781-00-2 (N_α-carbobenzyloxy-L-2-amino-3-acryloylamino)propionylglycine 
• 366781-04-6 N_α-carbobenzyloxy-L-2-amino-3-(oxiranecarbonylamino)propionic acid 
• 366780-96-3 (N_α-carbobenzyloxy-L-2-amino-3-acryloylamino)propionylglycine tert-butyl ester 

Relevant articles and documents

Structure-Activity Relationships of Potent, Targeted Covalent Inhibitors That Abolish Both the Transamidation and GTP Binding Activities of Human Tissue Transglutaminase

Human tissue transglutaminase (hTG2) is a multifunctional enzyme. It is primarily known for its calcium-dependent transamidation activity that leads to formation of an isopeptide bond between glutamine and lysine residues found on the surface of proteins, but it is also a GTP binding protein. Overexpression and unregulated hTG2 activity have been associated with numerous human diseases, including cancer stem cell survival and metastatic phenotype. Herein, we present a series of targeted covalent inhibitors (TCIs) based on our previously reported Cbz-Lys scaffold. From this structure-activity relationship (SAR) study, novel irreversible inhibitors were identified that block the transamidation activity of hTG2 and allosterically abolish its GTP binding ability with a high degree of selectivity and efficiency (kinact/KI > 105 M-1 min-1). One optimized inhibitor (VA4) was also shown to inhibit epidermal cancer stem cell invasion with an EC50 of 3.9 μM, representing a significant improvement over our previously reported "hit" NC9.

Synthesis of dipeptide-bound epoxides and α,β-unsaturated amides as potential irreversible transglutaminase inhibitors

Herein we report the synthesis of 24 novel peptides as potential irreversible inactivators of transglutaminase (TGase). These peptides were designed to resemble Cbz-L-Gly, known to be a good TGase substrate, and to include either α,β-unsaturated amide groups or the corresponding epoxide groups. The side chain length of the amino acid residue bearing the inhibitor group was also varied in order to permit investigation of this effect. Copyright