Solid-phase synthesis and circular dichroism study of β-abpeptoids
The development of peptidomimetic foldamers that can form well-defined folded structures is highly desirable yet challenging. We previously reported on α-ABpeptoids, oligomers of N-alkylated β2-homoalanines and found that due to the presence of chiral methyl groups at α-positions, α-ABpeptoids were shown to adopt folding conformations. Here, we report β-ABpeptoids having chiral methyl group at β-positions rather than α-positions as a different class of peptoids with backbone chirality. We developed a facile solid-phase synthetic route that enables the synthesis of β-ABpeptoid oligomers ranging from 2-mer to 8-mer in excellent yields. These oligomers were shown to adopt ordered folding conformations based on circular dichroism (CD) and NMR studies. Overall, these results suggest that β-ABpeptoids represent a novel class of peptidomimetic foldamers that will find a wide range of applications in biomedical and material sciences.
Sable, Ganesh A.,Lee, Kang Ju,Lim, Hyun-Suk
(2019/01/21)
An enantioselective synthesis of the topically-active carbonic anhydrase inhibitor MK-0507: 5,6-dihydro-(S)-4-(ethylamino)-(S)-6-methyl-4H-thieno[2,3-b]thiopyran- 2-sulfonamide 7,7-dioxide hydrochloride
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Blacklock,Sohar,Butcher,Lamanec,Grabowski
p. 1672 - 1679
(2007/10/02)
Stereochemical studies on the reactions catalyzed by the PLP-dependent enzyme 1-aminocyclopropane-1-carboxylate deaminase
The stereochemical course of 1-aminocyclopropane-1-carboxylate deaminase which catalyzes the fragmentation of the cyclopropane substrate to alpha -ketobutyrate and ammonia has been unraveled with the help of substrates stereospecifically labeled with deuterium and/or tritium, and this has afforded important information about the process occurring at the active site during enzymatic conversion.
Liu,Auchus,Walsh
p. 5335 - 5348
(2007/10/07)
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