115132-19-9

Usage

Chemical Properties

white powder or chunks

InChI:InChI=1/C15H21NO4/c1-10(11-8-6-5-7-9-11)12(13(17)18)16-14(19)20-15(2,3)4/h5-10,12H,1-4H3,(H,16,19)(H,17,18)/p-1/t10-,12-/m1/s1

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 59850-51-0 erythro-β-methylphenylalanine hydrochloride 

Downstream Products

• 133098-43-8 (4S,7R,13S)-13-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-3,3,14,14-tetramethyl-6,9,12-trioxo-7-((R)-1-phenyl-ethyl)-1,2-dithia-5,8,11-triaza-cyclotetradecane-4-carboxylic acid 
• 133098-42-7 (4S,7S,13S)-13-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-3,3,14,14-tetramethyl-6,9,12-trioxo-7-((S)-1-phenyl-ethyl)-1,2-dithia-5,8,11-triaza-cyclotetradecane-4-carboxylic acid 

Relevant academic research and scientific papers

Structure-Activity Study on the Phe Side Chain Arrangement of Endomorphins Using Conformationally Constrained Analogues

Structure-activity study on the Phe side chain arrangement of endomorphins using conformationally constrained analogues.Endomorphins-1 and -2 were substituted with all the beta-MePhe stereoisomers in their Phe residues to generate a conformationally constrained peptide set. This series of molecules was subjected to biological assays, and for beta-MePhe(4)-endomorphins-2, a conformational analysis was performed. Incorporation of (2S,3S)-beta-MePhe(4) resulted in the most potent analogues of both endomorphins with enhanced enzymatic stability. Their micro opioid affinities were 4-times higher than the parent peptides, they stimulated [(35)S]GTPgammaS binding, and they were found to be full agonists. NMR experiments revealed that C-terminal (2S,3S)-beta-MePhe in endomorphin-2 strongly favored the gauche (-) spatial orientation which implies the presence of the chi(1) = -60 degrees rotamer of Phe(4) in the binding conformer of endomorphins. Our results emphasize that the appropriate orientation of the C-terminal aromatic side chain of endomorphins is substantial for binding to the micro opioid receptor.

Side chain methyl substitution in the δ-opioid receptor antagonist TIPP has an important effect on the activity profile

The δ-opioid antagonist H-Tyr-Tic-Phe-Phe-OH (TIPP-OH) or its C- terminal amide analogue was systematically modified topologically by substitution of each amino acid residue by all stereoisomers of the corresponding β-methyl amino acid. The potency and se