205373-70-2

Upstream product

• 106-95-6 allyl bromide 
• 136159-65-4 (R)-4-benzyl-3-(3-phenyl-propionyl)-oxazolidin-2-one 
• 92576-42-6 2-benzyl-pent-4-enoyl chloride 
• 40217-17-2 (R)-4-(phenylmethyl)-2-oxazolidinone 
• 645-45-4 hydrocinnamic acid chloride 
• 501-52-0 3-Phenylpropionic acid 
• 6540-96-1 2-benzyl-4-pentenoic acid 

Downstream Products

• 133871-25-7 benzyl (R)-2-allyl-3-phenylpropanoate 
• 42361-59-1 (R)-2-phenylmethylpent-4-enoic acid 
• 131288-27-2 benzyl (S)-2-benzyl-3-formylpropanoate 

Relevant academic research and scientific papers

Structural requirements of histone deacetylase inhibitors: C4-modified saha analogs display dual HDAC6/HDAC8 selectivity

A compound having formula I for histone deacetylase inhibition is provided: or a pharmaceutically acceptable salt or hydrate thereof wherein R is alkyl, C6-18 aryl, C5-18 heteroaryl, C8-22 alkylaryl, C8-22 alkyl

The structural requirements of histone deacetylase inhibitors: C4-modified SAHA analogs display dual HDAC6/HDAC8 selectivity

Histone deacetylase (HDAC) enzymes govern the post-translational acetylation state of lysine residues on protein substrates, leading to regulatory changes in cell function. Due to their role in cancers, HDAC proteins have emerged as promising targets for

Fluorine-directed diastereoselective iodocyclizations

(Chemical Equation Presented) An inside job: β-Fluorinated lactones and tetrahydrofurans are synthesized by iodocyclization of various allylic fluorides. The fluorine substituent acts as a highly efficient syn-stereodirecting group for the ring closure. T

Stereochemistry in enzyme inhibition: Synthesis and evaluation of enantiomerically pure 2-benzyl-3-formylpropanoic acids as inhibitors of carboxypeptidase A

Both enantiomers of 2-benzyl-3-formylpropanoic acid were synthesized in five steps starting with hydrocinnamic acid and each enantiomer assayed for inhibitory activity against carboxypeptidase A to find that the (R)-form is 674-fold more potent than its e

A novel type of structurally simple nonpeptide inhibitors for α- chymotrypsin. Induced-fit binding of methyl 2-allyl-3-benzene-propanoate to the S2 subsite pocket

Unexpectedly, methyl and benzyl esters of 2-allyl-3-benzenepropanoic acid were found to be not substrates but potent competitive inhibitors for α-chymotrypsin. The inhibitory property of the structurally simple nonpeptidic compounds is ascribed to their high binding affinity to the enzyme at the S2 rather than S1 subsite pocket. These inhibitors exist in a flexible form in solution, but as they bind to the enzyme bulky contrained conformers present in a minute concentration play an important role, forming tighter enzyme-inhibitor complexes by binding to the large hydrophobic S2 pocket. The contrained conformers are thought to be resulted from intramolecular CH/π interactions between a vinylic proton and the aromatic π-electron cloud in the inhibitor molecules. These compounds constitute novel examples of the induced-fit binding inhibitor of possibly simplest structure.