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Stereoselective Synthesis of L-Deoxyaltronojirimycin from L-Serine
Rengasamy, Rajesh,Curtis-Long, Marcus J.,Ryu, Hyung-Won,Oh, Kyeong-Yeol,Park, Ki-Hun Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.7
(2S,3R)-3-Hydroxy-2-(hydroxymethyl)-3,6-dihydro-2H-pyridine 8, an important precursor for the synthesis of polyhydroxylated piperidine azasugars, has been prepared from L-serine. Highly stereoselective nucleophilic addition to amino aldehyde 5 gave the corresponding allylic alcohol 6 which proceeded to give dihydro-2H-piridine 7a via a Grubbs II catalyzed RCM. Stereoselective H-bond directed epoxidation of allylic alcohol led to the oxiranyl alcohol 9 which was easily converted to L-deoxyaltronojirimycin by regioselective ring opening.
Stereoselective Synthesis of L-Deoxyaltronojirimycin from L-Serine
Rajesh Rengasamy,Hyung Won Ryu,Kyeong Yeol Oh,박기훈,Marcus J. Curtis-Long 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.7
(2S,3R)-3-Hydroxy-2-(hydroxymethyl)-3,6-dihydro-2H-pyridine 8, an important precursor for the synthesis of polyhydroxylated piperidine azasugars, has been prepared from L-serine. Highly stereoselective nucleophilic addition to amino aldehyde 5 gave the corresponding allylic alcohol 6 which proceeded to give dihydro-2H-piridine 7a via a Grubbs II catalyzed RCM. Stereoselective H-bond directed epoxidation of allylic alcohol led to the oxiranyl alcohol 9 which was easily converted to L-deoxyaltronojirimycin by regioselective ring opening.
Cho, Jung-Keun,Rengasamy, Rajesh,Curtis-Long, Marcus John,Kim, Jin-Hyo,Lee, Ji-Won,Park, Ki-Hun The Korean Society for Applied Biological Chemistr 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.6
Azasugars derived from L-alanine and L-serine were screened for inhibitory activity against ${\alpha}$-rhamnosidase. The enantiomers of 1,6-dideoxynojirimycin ($ent$-1,6-dDNJ) (1) and ($2S$,$3R$)-2-(hydroxymethyl)piperidin-3-ol (5) showed highly specific and potent inhibition against ${\alpha}$-rhamnosidase with $K_i$ values of 4.2 and $16.6{\mu}M$, respectively. Structure of the best inhibitor features the same stereochemical configuration as L-rhamnose at C2, C3, and C4 centers. In kinetic studies, both compounds exhibited competitive inhibition behavior. Compound 1 manifested simple reversible slow-binding inhibition with the following kinetic parameters: ${\kappa}_3=1.17nM^{-1}\;min^{-1}$, ${\kappa}_4=5.96{\times}10^{-3}min^{-1}$, and $K_i^{app}$=5.1 mM.
Piperidine Azasugars Displaying Competitive α-Rhamnosidase Inhibition and their Kinetic Mechanism
Jung Keun Cho,Rajesh Rengasamy,Marcus John Curtis-Long,김진효,Ji Won Lee,박기훈 한국응용생명화학회 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.6
Azasugars derived from L-alanine and L-serine were screened for inhibitory activity against α-rhamnosidase. The enantiomers of 1,6-dideoxynojirimycin (ent-1,6-dDNJ) (1) and (2S,3R)-2-(hydroxymethyl)piperidin-3-ol (5) showed highly specific and potent inhibition against α-rhamnosidase with Ki values of 4.2 and 16.6 μM, respectively. Structure of the best inhibitor features the same stereochemical configuration as L-rhamnose at C2, C3, and C4 centers. In kinetic studies, both compounds exhibited competitive inhibition behavior. Compound 1 manifested simple reversible slow-binding inhibition with the following kinetic parameters: k3=1.17 nM−1 min−1, k4 = 5.96 ×10−3 min−1, and Ki app=5.1 mM.
Piperidine Azasugars Displaying Competitive α-Rhamnosidase Inhibition and their Kinetic Mechanism
( Ki Hun Park ),( Ji Won Lee ),( Jin Hyo Kim ),( Jung Keun Cho ),( Rajesh Rengasamy ),( Marcus John Curtis Long ) 한국응용생명화학회(구 한국농화학회) 2011 Applied Biological Chemistry (Appl Biol Chem) Vol.54 No.6
Azasugars derived from L-alanine and L-serine were screened for inhibitory activity against α- rhamnosidase. The enantiomers of 1,6-dideoxynojirimycin (ent-1,6-dDNJ) (1) and (2S,3R)-2- (hydroxymethyl)piperidin-3-ol (5) showed highly specific and potent inhibition against α- rhamnosidase with K i values of 4.2 and 16.6 μM, respectively. Structure of the best inhibitor features the same stereochemical configuration as L-rhamnose at C2, C3, and C4 centers. In kinetic studies, both compounds exhibited competitive inhibition behavior. Compound 1 manifested simple reversible slow-binding inhibition with the following kinetic parameters: k 3= 1.17 nM·1 min·1, k 4=5.96 ×10·3 min·1, and K i app=5.1 mM.
Linoleic Acid from Bamboo (Phyllostachys Bambusoides) Displaying Potent α- Glucosidase Inhibition
Sunin Jung(정성인),Su Tae Kang(강수태),Cheol Yong Choi(최철용),Kyeong Yeol Oh(오경열),Jung Keun Cho(조정근),Rajesh Rengasamy,Ki Hun Park(박기훈) 한국생명과학회 2009 생명과학회지 Vol.19 No.5
당가수분해효소 저해제는 2형 당뇨병, 암, 바이러스 감염제 개발의 주요 타켓화합물이 되고 있다. 본 연구에서는 기능성식품 소재로 이용될 수 있는 대나무 잎에서 α-glucosidase 저해제를 탐색하였다. 대나무 잎을 메탄올 용매로 추출하고, 이들을 핵산, 클로로포름, 부탄올로 용매분획 하였다. 용매 분획된 각 추출물의 α-glucosidase 저해활성을 검정시험에서 핵산 분획층에서 강한 α-glucosidase 저해활성(IC50 33.5 ㎍/ml)을 관찰하였다. 높은 저해활성을 보여준 핵산 분획층의 활성물질은 linoleic acid로 구조동정 되었다. 분리된 linoleic acid는 IC50이 12.4 ㎛로 높은 α-glucosidase 저해활성을 나타내었다. 저해활성 메커니즘 연구에서 linoleic acid는 비경쟁적 저해 양상을 나타내었다. 본 연구는 대나무가 α-glucosidase 저해활성을 나타내는 첫 번째 연구 결과이다. Glycosidase inhibitors are major targets in the treatment of type Ⅱ diabetes, cancer and viral infections. This study was carried out to investigate the glycosidase inhibitory substances from bamboo (Phyllostachys bambusoides). Bamboo was extracted with methanol and then further fractionated with n-hexane, chloroform, n-BuOH and aqueous to get an active fraction. All extracts were evaluated for α-glucosidase inhibitory activities to identify the n-hexane fraction with 33.5 ㎍/ml of IC50 value. Active compound 1 in the n-hexane fraction was identified as linoleic acid, which exhibited inhibitory activity with 12.4 ㎛ of IC50 value. Mechanistic analysis showed that linoleic acid exhibited noncompective inhibition. This is the first study in which bamboo is reported to show α-glucosidase inhibitory activity.