57022-32-9

Usage

Structure

Piperazinedione derivative with a 4-aminobutyl group attached to the third carbon atom

Stereoisomeric form

(S)-(9CI)

Usage

Building block for the synthesis of various bioactive compounds and potential drug candidates in pharmaceutical research and development

Versatility

The chemical structure and functional groups make it a versatile intermediate in organic synthesis and medicinal chemistry.

Upstream product

• 2389-45-9 Boc-Lys(Z)-OH 
• 33043-26-4 N-(N^α-tert-butoxycarbonyl-N^ε-carbobenzoxy-L-lysyl)glycine ethyl ester 
• 63276-43-7 N-6-Benzyloxycarbonyl-L-lysyl>-glycin-methylester 
• 23234-35-7 N^α tert-Butyloxycarbonyl-N^ε-carbobenzyloxy-L-lysyl-glycine methyl ester 
• 34404-36-9 Boc-Lys(Z)-OSu 
• 84624-27-1 Boc-Lys(Fmoc)-OH 
• 911664-89-6 Z-Lys(Z)-Gly-OMe 

Relevant academic research and scientific papers

ADVANCED GLYCATION END-PRODUCT BREAKING BIOCATALYSTS

In various aspects and embodiments the invention provides compositions and methods for removing glucosepane from one or more proteins in a subject. In certain embodiments, the method comprises administering to the subject an effective amount of a polypept

PIPERAZINE-2,5-DIONES AS TGF-BETA INHIBITORS

The present disclosure is concerned with piperazine-2,5-diones that are capable of inhibiting TGF-β and methods of treating cancers such as, for example, multiple myeloma and a hematologic malignancy, and methods of treating fibrotic conditions using these compounds. This abstract is intended as a scanning tool for purposes of searching in the particular art and is not intended to be limiting of the present invention.

Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the "selectivity Pocket", Substrate-Binding Site, and NAD+-Binding Site

The NAD+-dependent deacetylase SIRT2 represents an attractive target for drug development. Here, we designed and synthesized drug-like SIRT2-selective inhibitors based on an analysis of the putative binding modes of recently reported SIRT2-selective inhibitors and evaluated their SIRT2-inhibitory activity. This led us to develop a more drug-like diketopiperazine structure as a "hydrogen bond (H-bond) hunter" to target the substrate-binding site of SIRT2. Thioamide 53, a conjugate of diketopiperazine and 2-anilinobenzamide which is expected to occupy the "selectivity pocket" of SIRT2, exhibited potent SIRT2-selective inhibition. Inhibition of SIRT2 by 53 was mediated by the formation of a 53-ADP-ribose conjugate, suggesting that 53 is a mechanism-based inhibitor targeting the "selectivity pocket", substrate-binding site, and NAD+-binding site. Furthermore, 53 showed potent antiproliferative activity toward breast cancer cells and promoted neurite outgrowth of Neuro-2a cells. These findings should pave the way for the discovery of novel therapeutic agents for cancer and neurological disorders.

A Mechanism for bitter Taste Sensibility in Peptides

To estimate the steric distance between the bitter taste determinant sites in peptides, some cyclic dipeptides, amino acid anilides, amino acid cyclohexylamides, and benzoyl amino acids were synthesized and their tastes were evaluated.The diketopiperazine ring of cyclic dipeptides acted as a bitter taste determinant site due to its hydrophobicity.The steric distance between 2 sites was estimated as 4.1 Angstroem from the molecule models of cyclic dipeptides composed of typical amino acids in the bitter peptides.Due to the hypothesis of two bitter taste determinant sites, which bind with the bitter taste receptor via a "binding unit" and a "stimulating unit," a mechanism for the bitterness in peptides was postulated.