92010-16-7

Basic information

• Product Name: L-Proline, 1-(3,3-dimethyl-1-oxobutyl)-, phenylmethyl ester
• CAS NO: 92010-16-7
• Molecular Formula: C18H25NO3
• Molecular Weight: 303.401
• Mol File: 92010-16-7.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: L-Proline, 1-(3,3-dimethyl-1-oxobutyl)-, phenylmethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: L-Proline, 1-(3,3-dimethyl-1-oxobutyl)-, phenylmethyl ester(92010-16-7)
• EPA Substance Registry System: L-Proline, 1-(3,3-dimethyl-1-oxobutyl)-, phenylmethyl ester(92010-16-7)

Safety Data

• Hazardous Substances Data: 92010-16-7(Hazardous Substances Data)

Upstream product

• 1070-83-3 tert-Butylacetic acid 
• 41324-66-7 H-Pro-OBzl 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 

Downstream Products

• 92010-19-0 (S)-1-(3,3-Dimethyl-butyryl)-pyrrolidine-2-carboxylic acid 2-carboxy-phenyl ester 
• 92010-18-9 (S)-1-(3,3-Dimethyl-butyryl)-pyrrolidine-2-carboxylic acid 2-benzyloxycarbonyl-phenyl ester 

Relevant articles and documents

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.

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