874162-95-5

Upstream product

• 89813-47-8 N-(tert-butoxycarbonyl)-(2S,4R)-4-hydroxyproline benzyl ester 

Downstream Products

• 132622-69-6 (2S,4R)-4-amino-1-(tert-butoxycarbonyl)pyrrolidine-2-carboxylic acid 
• 874163-11-8 3(R)-[(4(R)-((4-azido-2-hydroxy-5-iodobenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-10-7 3(R)-[(4(R)-((4-azido-2-hydroxybenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-09-4 3(R)-[(4(R)-((4-azidobenzoyl)amino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-03-8 methyl 3(R)-[(4(R)-(4-benzyloxycarbonylamino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetate 
• 874163-05-0 3(R)-[(4(R)-(4-benzyloxycarbonylamino)-1-(tert-butoxycarbonyl)-2(S)-pyrrolidinylcarbonyl)amino]-2-oxo-1-pyrrolidineacetamide 
• 874163-00-5 (2S,4R)-1-(tert-butoxycarbonyl)-4-(N-benzyloxycarbonyl)aminoproline 
• 185304-19-2 (2S,4R)-2-benzyl 1-tert-butyl 4-azidopyrrolidine-1,2-dicarboxylate 

Relevant academic research and scientific papers

Discovery of subnanomolar arginine-glycine-aspartate-based αvβ3/αvβ5 integrin binders embedding 4-aminoproline residues

The embodiment of 4-aminoproline residues (Amp) into the arginine-glycine-aspartate (RGD) sequence led to the discovery of a novel class of high-affinity αvβ3/αvβ 5 integrin binders [IC50h(αvβ 3) 0.03-5.12 nM; IC50h(αvβ 5) 0.88-154 nM]. A total of eight cyclopeptides of type cyclo-[-Arg-Gly-Asp-Amp-], 5-12, were assembled by a standard solid-phase peptide synthesis protocol that involved the C2-carboxyl and C4-amino functionalities of the proline scaffolds, leaving the Nα- nuclear site untouched. Functionalization of this vacant proline site with either alkyl or acyl substituents proved feasible, with significant benefit to the integrin binding capabilities of the ligands. Notably, six out of eight cyclopeptide inhibitors, 5-7 and 9-11, showed moderate yet significant selectivity toward the αvβ3 receptor. The three-dimensional structure in water was determined by NMR techniques and molecular dynamics calculations. Docking studies to the X-ray crystal structure of the extracellular segment of integrin αvβ3 complexed with reference compound 1 were also performed on selected analogues to highlight the structural features required for potent ligand binding affinity.

Design and synthesis of photoaffinity-labeling ligands of the L-prolyl-L-leucylglycinamide binding site involved in the allosteric modulation of the dopamine receptor

Pro-Leu-Gly-NH2 (PLG), in addition to its endocrine effects, possesses the ability to modulate dopamine 02 receptors within the central nervous system. However, the precise binding site of PLG is unknown. Potential photoaffinity-labeling ligand