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Go Heum Yeun,Seung Hwan Lee,Yong Bae Lim,Hye Sook Lee,원무호,이봉호,박정호 대한화학회 2013 Bulletin of the Korean Chemical Society Vol.34 No.4
In the previous paper (Bull. Korean Chem. Soc., 2011, 32, 2997), the hybrid molecules between α-lipoic acid (ALA) and polyphenols (PPs) connected with neutral 2-(2-aminoethoxy)ethanol linker (linker-1) showed new biological activity such as butyrylcholinesterase (BuChE) inhibition. In order to increase the binding affinity of the hybrid compounds to cholinesterase (ChE), the neutral 2-(2-aminoethoxy)ethanol (linker 1) was switched to the cationic 2-(piperazin-1-yl)ethanol linker (linker 2). The IC50 values of the linker-2 hybrid molecules for BuChE inhibition were lower than those of linker-1 hybrid molecules (except 9-2) and they also had the same great selectivity for BuChE over AChE (> 800 fold) as linker-1 hybrid molecules. ALA-acetyl caffeic acid (10- 2, ALA-AcCA) was shown as an effective inhibitor of BuChE (IC50 = 0.44 ± 0.24 μM). A kinetic study using 7- 2 showed that it is the same mixed type inhibition as 7-1. Its inhibition constant (Ki) to BuChE is 4.3 ± 0.09 μM.
Yeun, Go Heum,Lee, Seung Hwan,Lim, Yong Bae,Lee, Hye Sook,Won, Moo-Ho,Lee, Bong Ho,Park, Jeong Ho Korean Chemical Society 2013 Bulletin of the Korean Chemical Society Vol.34 No.4
In the previous paper (Bull. Korean Chem. Soc., 2011, 32, 2997), the hybrid molecules between ${\alpha}$-lipoic acid (ALA) and polyphenols (PPs) connected with neutral 2-(2-aminoethoxy)ethanol linker (linker-1) showed new biological activity such as butyrylcholinesterase (BuChE) inhibition. In order to increase the binding affinity of the hybrid compounds to cholinesterase (ChE), the neutral 2-(2-aminoethoxy)ethanol (linker 1) was switched to the cationic 2-(piperazin-1-yl)ethanol linker (linker 2). The $IC_{50}$ values of the linker-2 hybrid molecules for BuChE inhibition were lower than those of linker-1 hybrid molecules (except 9-2) and they also had the same great selectivity for BuChE over AChE (> 800 fold) as linker-1 hybrid molecules. ALA-acetyl caffeic acid (10-2, ALA-AcCA) was shown as an effective inhibitor of BuChE ($IC_{50}=0.44{\pm}0.24{\mu}M$). A kinetic study using 7-2 showed that it is the same mixed type inhibition as 7-1. Its inhibition constant (Ki) to BuChE is $4.3{\pm}0.09{\mu}M$.
Selective Butyrylcholinesterase Inhibitors Using Polyphenol-polyphenol Hybrid Molecules
Woo, Yeun-Ji,Lee, Bo-Hyun,Yeun, Go-Heum,Kim, Hyun-Ju,Won, Moo-Ho,Kim, Sang-Hern,Lee, Bong-Ho,Park, Jeong-Ho Korean Chemical Society 2011 Bulletin of the Korean Chemical Society Vol.32 No.8
Polyphenols (PPs) are known as antioxidant compounds having benign biological activities. In this paper, a series of hybrid molecules between the free or acetyl protected polyphenol compounds were synthesized and their in vitro antioxidant activity (DPPH assay) and cholinesterase [acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)] inhibition activities were evaluated. As expected, free phenolic hybrid compounds (6 and 8) showed better antioxidant activity than acetyl protected hybrid compounds (5 and 7) from DPPH assay. But the contrast result was obtained from BuChE inhibition assay. Acetyl protected hybrid compounds (5 and 7) showed better inhibition activity for BuChE than free phenolic hybrid compounds (6 and 8). Specifically, 10 (AcFA-AcFA) were shown as an effective inhibitor of BuChE ($IC_{50}=2.3{\pm}0.3{\mu}M$) and also had a great selectivity for BuChE over AChE (more than 170 fold). Inhibition kinetic studies with acetyl protected compounds (5, 7, 9, and 10) indicated that 5, 7 and 10 are a hyperbolic mixed-type inhibition and 10 is a competitive inhibition type. The binding affinity (Ki) value of 10 to BuChE is $2.32{\pm}0.15{\mu}M$.
Selective Butyrylcholinesterase Inhibitors Using Polyphenol-polyphenol Hybrid Molecules
Yeun Ji Woo,Bo Hyun Lee,Go Heum Yeun,Hyun Ju Kim,원무호,김상헌,이봉호,박정호 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.8
Polyphenols (PPs) are known as antioxidant compounds having benign biological activities. In this paper, a series of hybrid molecules between the free or acetyl protected polyphenol compounds were synthesized and their in vitro antioxidant activity (DPPH assay) and cholinesterase [acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)] inhibition activities were evaluated. As expected, free phenolic hybrid compounds (6 and 8) showed better antioxidant activity than acetyl protected hybrid compounds (5 and 7) from DPPH assay. But the contrast result was obtained from BuChE inhibition assay. Acetyl protected hybrid compounds (5 and 7) showed better inhibition activity for BuChE than free phenolic hybrid compounds (6 and 8). Specifically, 10 (AcFA-AcFA) were shown as an effective inhibitor of BuChE (IC_50 = 2.3 ± 0.3 μM) and also had a great selectivity for BuChE over AChE (more than 170 fold). Inhibition kinetic studies with acetyl protected compounds (5, 7, 9, and 10) indicated that 5, 7 and 10 are a hyperbolic mixed-type inhibition and 10is a competitive inhibition type. The binding affinity (Ki) value of 10 to BuChE is 2.32 ± 0.15 μM.
Woo, Yeun-Ji,Lee, Bo-Hyun,Yeun, Go-Heum,Kim, Hyun-Ju,Ko, Jang-Myoun,Won, Moo-Ho,Lee, Bong-Ho,Park, Jeong-Ho Korean Chemical Society 2011 Bulletin of the Korean Chemical Society Vol.32 No.suppl8
A series of hybrid molecules between (R)-lipoic acid (ALA) and the acetylated or methylated polyphenol compounds were synthesized and their in vitro cholinesterase [acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)] inhibition activities were checked. The $IC_{50}$ values of all hybrid molecules for a BuChE inhibition were lower than those of the single parent compounds. Specifically, ALA-acetyl protected caffeic acid (11, ALA-AcCA) was shown as an effective inhibitor of BuChE ($IC_{50}=0.5{\pm}0.2\;{\mu}M$) and also had a great selectivity for BuChE over AChE (more than 800 fold). Inhibition kinetic study indicated that 11 is a mixed inhibition type. Its binding affinity ($K_i$) value to BuChE is $1.52{\pm}0.18\;{\mu}M$.
Yeun Ji Woo,Bo Hyun Lee,Go Heum Yeun,Hyun Ju Kim,고장면,원무호,이봉호,박정호 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.8
A series of hybrid molecules between (R)-lipoic acid (ALA) and the acetylated or methylated polyphenol compounds were synthesized and their in vitro cholinesterase [acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)] inhibition activities were checked. The IC_50 values of all hybrid molecules for a BuChE inhibition were lower than those of the single parent compounds. Specifically, ALA-acetyl protected caffeic acid (11,ALA-AcCA) was shown as an effective inhibitor of BuChE (IC_50 = 0.5 ± 0.2 μM) and also had a great selectivity for BuChE over AChE (more than 800 fold). Inhibition kinetic study indicated that 11 is a mixed inhibition type. Its binding affinity (Ki) value to BuChE is 1.52 ± 0.18 μM.
Yang, Kye Yong,Park, Yun Heum,Go, Kyung Chan TaylorFrancis 2006 Molecular Crystals and Liquid Crystals Vol.445 No.1
<P>Poly(vinyl phenylmethylamine) (PVPMA) and poly(vinyl benzlmethylyamine) (PVBMA) were chemically synthesized and PVPMA/polyaniline (PANI) and PVBMA/PANI composites were electrochemically prepared for the investigation of the effect of different bulky side groups of matrix polymers on the electrochemical properties of the polymer composites. The cyclic voltammertry, chronoamperomtry, and conductivity were investigated.</P>