80887-21-4

Upstream product

• 13633-25-5 1-Bromo-4-phenylbutane 
• 1068-90-2 2-acetylaminomalonic acid diethyl ester 
• 3360-41-6 4-phenyl-butan-1-ol 
• 65512-08-5 4-phenylbutyl methanesulfonate 
• 64283-87-0 4-phenyl-1-iodobutane 

Downstream Products

• 1316742-26-3 2-(RS)-(2-aminobenzoylamino)-6-phenylhexanoic acid ethyl ester 
• 1316742-36-5 2-(RS)-{2-[(1H-indole-2-carbonyl)amino]benzoylamino}-6-phenylhexanoic acid ethyl ester 
• 1316741-79-3 2-(RS)-{2-[(1H-indole-2-carbonyl)amino]benzoylamino}-6-phenylhexanoic acid 
• 1316742-08-1 2-(RS)-amino-6-phenylhexanoic acid hydrochloride 
• 1316742-15-0 2-(RS)-amino-6-phenylhexanoic acid ethyl ester hydrochloride 
• 150722-87-5 Boc-Nle-(S)-β-homo-Aph-OBzl 
• 150722-86-4 Boc-Nle-(R)-β-homo-Aph-OBzl 
• 150722-83-1 (S)-benzyl 2<(tert-butyloxycarbonyl)amino>-7-phenylheptanoate 
• 150722-82-0 (R)-benzyl 2<(tert-butyloxycarbonyl)amino>-7-phenylheptanoate 
• 150722-70-6 (S)-2<(tert-butyloxycarbonyl)amino>-7-phenylheptanoic acid 
• 150722-69-3 (R)-2<(tert-butyloxycarbonyl)amino>-7-phenylheptanoic acid 

Relevant academic research and scientific papers

NEOSEPTINS: SMALL MOLECULE ADJUVANTS

A MD-2:TLR4 complex agonist compound is disclosed whose structure corresponds to Formula (I), as defined within. Also disclosed are a method of its preparation and use, as well as a pharmaceutical composition containing the same.

New anthranilic acid based antagonists with high affinity and selectivity for the human cholecystokinin receptor 1 (hCCK1-R)

The anthranilic acid diamides represent the most recent class of nonpeptide CCK1 receptor (CCK1-R) antagonists. Herein we describe the second phase of the anthranilic acid C-terminal optimization using nonproteinogenic amino acids containing a phenyl ring in their side chain. The Homo-Phe derivative 2 (VL-0797) enhanced 12-fold the affinity for the rat CCK1-R affinity and 15-fold for the human CCK1-R relative to the reference compound 12 (VL-0395). The eutomer of 2 (6) exhibited a nanomolar range affinity toward the human CCK1-R and was at least 400-fold selective for the CCK1-R over the CCK2-R. Molecular docking in the modeled CCK1-R and its validation by site-directed mutagenesis experiments showed that the 6 binding site overlaps that occupied by the C-terminal bioactive region of the natural agonist CCK. Owing to their interesting properties, new compounds provided by this study represent a solid basis for further advances aimed at synthesis of clinically valuable CCK1-R antagonists.

Synthesis and biological evaluation of cholecystokinin analogs in which the Asp-Phe-NH2 moiety has been replaced by a 3-amino-7-phenylheptanoic acid or a 3-amino-6-(phenyloxy)hexanoic acid

Boc-Tyr(SO3H)-Nle-Gly-Trp-Nle-Asp-2-phenylethyl ester (JMV180), an analog of the C-terminal octapeptide of cholecystokinin (CCK-8), shows interesting biological activities behaving as an agonist at the high-affinity CCK binding sites and as an