73030-06-5

Basic information

• Product Name: L-Proline, 1-(1-oxo-3-phenylpropyl)-
• CAS NO: 73030-06-5
• Molecular Formula: C14H17NO3
• Molecular Weight: 247.294
• Mol File: 73030-06-5.mol

Chemical Properties

• CAS DataBase Reference: L-Proline, 1-(1-oxo-3-phenylpropyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Proline, 1-(1-oxo-3-phenylpropyl)-(73030-06-5)
• EPA Substance Registry System: L-Proline, 1-(1-oxo-3-phenylpropyl)-(73030-06-5)

Safety Data

• Hazardous Substances Data: 73030-06-5(Hazardous Substances Data)

Upstream product

• 645-45-4 hydrocinnamic acid chloride 
• 147-85-3 L-proline 
• 501-52-0 3-Phenylpropionic acid 
• 88105-74-2 (S)-1-(3-phenyl-propionyl)-pyrrolidine-2-carboxylic acid benzyl ester 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 

Downstream Products

• 76084-36-1 1-((R)-2-Isocyanato-pyrrolidin-1-yl)-3-phenyl-propan-1-one 
• 92010-15-6 (S)-1-(3-Phenyl-propionyl)-pyrrolidine-2-carboxylic acid 2-carboxy-phenyl ester 
• 125792-32-7 3-Phenylpropionyl-Pro-pyrrolidine 
• 151647-54-0 3-phenyl-1-pyrrolidin-1-yl-propane-1-one 
• 88130-50-1 N-(3-phenylpropanoyl)-L-prolyl-DL-α-methylphenylalanyl-N^ω-nitro-L-arginine 
• 88084-36-0 N-(3-phenylpropanoyl)-L-prolyl-DL-α-methylphenylalanyl-L-arginine 

Relevant articles and documents

2-Imidazole as a Substitute for the Electrophilic Group Gives Highly Potent Prolyl Oligopeptidase Inhibitors

Different five-membered nitrogen-containing heteroaromatics in the position of the typical electrophilic group in prolyl oligopeptidase (PREP) inhibitors were investigated and compared to tetrazole. The 2-imidazoles were highly potent inhibitors of the pr

Modulating hydrogen-bond basicity within the context of protein-ligand binding: A case study with thrombin inhibitors that?reveals a dominating role for desolvation

Understanding subtle aspects of hydrogen bonding is a challenging but crucial task to improve our ability to design ligands with high affinity for protein hosts. To gain a deeper understanding of these aspects, we investigated a series of thrombin inhibitors in which the basicity of the ligand's group that accepts an H-bond from Gly216 was modulated via bioisosterism; e.g., a C=O acceptor was made electron deficient or rich via bioisosteric replacements of the adjacent moiety. Although the ligand's binding affinity was anticipated to improve when the H-bond basicity is increased (due to stronger H-bonding with the protein), we herein present data that unexpectedly revealed an opposite trend. This trend was attributed to a dominating role played by desolvation in determining the relative binding affinity. For example, a decrease in the H-bond basicity reduces the desolvation penalty and, as experimentally observed, improves the binding affinity, given that the reduction in the desolvation penalty dominates the change in the net contribution of the ligand's interactions with the protein. The current study, therefore, reveals that desolvation can be a major underlying cause for the apparently counterintuitive structure-activity relationship (SAR) outcomes, and indicates that understanding this factor can improve our ability to predict binding affinity and to design more potent ligands.

Reductive ipso-radical cyclization onto aromatic rings of five-membered alicyclic amino acids bearing N-(2-phenyl)benzoyl groups by photoinduced electron transfer promoted decarboxylation

A new radical cyclization has been developed for the one-step synthesis of spiro dihydroisoquinolinone derivatives from alicyclic amino acids bearing N-(2-phenyl)benzoyl groups through photoinduced electron transfer (PET)-promoted decarboxylation. Reductive ipso-radical cyclization onto a benzene ring by an alkyl radical is achieved under mild conditions for the first time, although the substrates are limited to five-membered aliphatic carboxylic acids bearing N-(2-phenyl)benzoyl groups.

An improved large scale procedure for the preparation of N-Cbz amino acids

A simple and scalable method for the preparation of N-Cbz protected amino acids is presented which uses a mixture of aqueous sodium carbonate and sodium bicarbonate to maintain the appropriate pH during the addition of benzyl chloroformate. The method has been extended to other N-protections and is amenable to large scale preparation of an intermediate toward Zofenopril, an ACE inhibitor.

Enhancement of hydrophobic interactions and hydrogen bond strength by cooperativity: Synthesis, modeling, and molecular dynamics simulations of a congeneric series of thrombin inhibitors

Accurately predicting the binding affinity of ligands to their receptors by computational methods is one of the major challenges in structure-based drug design. One of the potentially significant errors in these predictions is the common assumption that the ligand binding affinity contributions of noncovalent interactions are additive. Herein we present data obtained from two separate series of thrombin inhibitors containing hydrophobic side chains of increasing size that bind in the S3 pocket and with, or without, an adjacent amine that engages in a hydrogen bond with Gly 216. The first series of inhibitors has a m-chlorobenzyl moiety binding in the S1 pocket, and the second has a benzamidine moiety. When the adjacent hydrogen bond is present, the enhanced binding affinity per ?2 of hydrophobic contact surface in the S3 pocket improves by 75% and 59%, respectively, over the inhibitors lacking this hydrogen bond. This improvement of the binding affinity per ?2 demonstrates cooperativity between the hydrophobic interaction and the hydrogen bond.

Characterization of the binding properties of SIRT2 inhibitors with a N-(3-phenylpropenoyl)-glycine tryptamide backbone

SIRT2 inhibitors with a N-(3-phenylpropenoyl)-glycine tryptamide backbone were studied. This backbone has been developed in our group, and it is derived from a compound originally found by virtual screening. In addition, compounds with a smaller 3-phenylpropenoic acid tryptamide backbone were also included in the study. Binding modes for the new compounds and the previously reported compounds were analyzed with molecular modelling methods. The approach, which included a combination of molecular dynamics, molecular docking and cluster analysis, showed that certain docking poses were favourable despite the conformational variation in the target protein. The N-(3-phenylpropenoyl)-glycine tryptamide backbone is also a good backbone for SIRT2 inhibitors, and the series of compounds includes several potent SIRT2 inhibitors.

Proline derivatives possessing prolyl endopeptidase-inhibitory activity

Novel proline derivatives of the following formula (I) STR1 wherein each symbol is as defined in the specification, which specifically inhibit prolyl endopeptidase activity and can be used for the prevention and/or treatment of dementia and amnesia as agents which act directly on the central symptoms of dementia.

4H-3,1-benzoxazin-4-one derivative

4H-3,1-benzoxazin-4-one derivatives represented by formula (I) below: STR1 wherein R1 represents a lower alkyl group, R2 represents a lower alkyl group, a lower alkylthioalkyl group, or a lower alkanesulfinylalkyl group, R3/sup

Design, synthesis, and testing of potential antisickling agents. 5. Disubstituted benzoic acids designed for the donor site and proline salicylates designed for the acceptor site

This paper reports the discovery of a new class of potent antigelling agents. The new compounds, disubstituted benzoic acid derivatives, were designed by using molecular modeling experiments. These molecules contain functional groups positioned to interac