15327-02-3Relevant academic research and scientific papers
Synthesis and olfactory evaluation of optically active β-alkyl substituted γ-lactones and whiskey lactone analogues
Kato, Daiki,Kawasaki, Masashi,Morita, Yuko,Okada, Takuya,Tanaka, Yasuo,Toyooka, Naoki
, (2020/02/22)
Optically active β-alkyl substituted γ-lactones and whiskey lactone analogues were synthesized, and the odor properties were evaluated. During the preparation of the chiral intermediates, we found good reaction conditions for the highly enantioselective esterification of 3-arylmethyl-2-methyl-1-propanols to kinetically resolve them. The results of the olfactory evaluations of the synthesized lactones revealed that the alkyl groups on the γ-lactone rings played an important role for the odor profiles.
A Desulfurative Strategy for the Generation of Alkyl Radicals Enabled by Visible-Light Photoredox Catalysis
Xue, Fei,Wang, Falu,Liu, Jiazhen,Di, Jiamei,Liao, Qi,Lu, Huifang,Zhu, Min,He, Liping,He, Huan,Zhang, Dan,Song, Hao,Liu, Xiao-Yu,Qin, Yong
supporting information, p. 6667 - 6671 (2018/06/11)
Herein, we present a new desulfurative method for generating primary, secondary, and tertiary alkyl radicals through visible-light photoredox catalysis. A process that involves the generation of N-centered radicals from sulfinamide intermediates, followed by subsequent fragmentation, is critical to forming the corresponding alkyl radical species. This strategy has been successfully applied to conjugate addition reactions that features mild reaction conditions, broad substrate scope (>60 examples), and good functional-group tolerance.
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
Kim, Dong H.,Li, Zhi-Hong,Lee, Soo Suk,Park, Jeong-Il,Chung, Sang J.
, p. 239 - 249 (2007/10/03)
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.
