23500-13-2

Basic information

• Product Name: 1-(1-oxobutyl)-L-proline
• Synonyms: 1-(1-oxobutyl)-L-proline;Einecs 245-696-9;(2S)-1-(1-oxobutyl)-2-pyrrolidinecarboxylic acid;(2S)-1-butanoylpyrrolidine-2-carboxylic acid;(2S)-1-butyrylproline;1-butyrylproline
• CAS NO: 23500-13-2
• Molecular Formula: C₉H₁₅NO₃
• Molecular Weight: 185.2203
• EINECS: 245-696-9
• Mol File: 23500-13-2.mol
• Article Data: 7

Chemical Properties

• Boiling Point: 378.5 °C at 760 mmHg
• Flash Point: 182.7 °C
• Appearance: /
• Density: 1.185 g/cm³
• Vapor Pressure: 8.96E-07mmHg at 25°C
• Refractive Index: 1.508
• CAS DataBase Reference: 1-(1-oxobutyl)-L-proline(CAS DataBase Reference)
• NIST Chemistry Reference: 1-(1-oxobutyl)-L-proline(23500-13-2)
• EPA Substance Registry System: 1-(1-oxobutyl)-L-proline(23500-13-2)

Safety Data

• Hazardous Substances Data: 23500-13-2(Hazardous Substances Data)

Usage

General Description

1-(1-oxobutyl)-L-proline is a chemical compound with the molecular formula C9H15NO3. It is also known as N-(1-oxobutyl)-L-proline or N-butyryl-L-proline. 1-(1-oxobutyl)-L-proline is a derivative of the amino acid proline and is often used in organic synthesis and pharmaceutical research. It has the potential to act as a building block for the synthesis of various biologically active compounds. Additionally, 1-(1-oxobutyl)-L-proline has been studied for its potential pharmacological activities, including its anti-inflammatory and analgesic properties. Overall, this compound has various potential applications in the pharmaceutical and chemical industries due to its unique chemical structure and properties.

InChI:InChI=1/C9H15NO3/c1-2-4-8(11)10-6-3-5-7(10)9(12)13/h7H,2-6H2,1H3,(H,12,13)

Upstream product

• 84520-92-3 (S)-benzyl 1-butyrylpyrrolidine-2-carboxylate 
• 41324-66-7 H-Pro-OBzl 
• 141-75-3 butyryl chloride 
• 147-85-3 L-proline 
• 70741-39-8 2,5-dioxopyrrolidin-1-yl butyrate 
• 107-92-6 butyric acid 

Downstream Products

• 1215172-65-8 C₂₅H₃₀N₄O₄ 

Relevant articles and documents

Nocardiopsins C and D and nocardiopyrone A: New polyketides from an Australian marine-derived Nocardiopsis sp.

A Nocardiopsis sp. (CMB-M0232) recovered from marine sediment collected off the coast of South Molle Island, Queensland, Australia, yielded two new examples of rare prolinyl-macrolactam polyketides, nocardiopsins C (1) and D (2), a new highly substituted α-pyrone polyketide, nocardiopyrone A (3), and the previously reported macrolide polyketides nocardiopsins A (4) and B (5). Structures were assigned on the basis of detailed spectroscopic analysis, degradation, and chemical derivatization. PCR amplification of CMB-M0232 genomic DNA revealed the presence of type I and type II polyketide synthase and nonribosomal peptide synthase domains. 2012 Elsevier Ltd. All rights reserved.

Synthesis of the peptaibol framework of the anticancer agent culicinin D: Stereochemical assignment of the AHMOD moiety

The postulated structure of the potent anticancer peptaibol culicinin D has been synthesized using Fmoc-based solid-phase peptide synthesis (SPPS). Comparison of the 1H NMR data for the reported structure of culicinin D with the data obtained for the two synthetic polypeptides epimeric at C-6 in the AHMOD unit established the C-6 stereochemistry of the AHMOD residue in the natural product to be (R).

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.