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Lawrence H. Lazarus - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of Stereoisomeric Analogues of Endomorphin-2, H-Tyr-Pro-Phe-Phe-NH2, and Examination of Their Opioid Receptor Binding Activities and Solution Conformation
Biochemical and biophysical research communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH(2)) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar mu- and delta-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d-amino acid isomers exhibited lower interaction with mu-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l-configuration was the most suitable for Binding within the mu Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for mu-Receptor-Binding sites.
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synthesis of stereoisomeric analogues of endomorphin 2 h tyr pro phe phe nh2 and examination of their opioid Receptor Binding activities and solution conformation
Biochemical and Biophysical Research Communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:Abstract All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar μ- and δ-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d -amino acid isomers exhibited lower interaction with μ-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l -configuration was the most suitable for Binding within the μ Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for μ-Receptor-Binding sites.
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amino acids and peptides lvi synthesis of pyrazinone ring containing opioid mimetics and examination of their opioid Receptor Binding Activity
Tetrahedron, 1999Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Junpei Yamazaki, Lawrence H. LazarusAbstract:Abstract Cyclization of dipeptidyl chloromethyl ketones gave 6-(4-aminobutyl)-3-carboxyethyl-5-methyl-2(1H)-pyrazinone (3), 3-(4-aminobutyl)-6-carboxyethyl-5-methyl-2(1H)-pyrazinone (6), and 3,6-bis(4-aminobutyl)-5-methyl-2(1H)-pyrazinone (15). Using above pyrazinone derivatives, three opioid mimetics were prepared (III-V). Derivatives containing 3 and 6 demonstrated weak μ and δ-opioid Receptor affinities ranging from 1.6 mM to 4.1 mM while the opioid mimetic containing derivative 15 displayed higher μ-opioid Receptor Binding affinity (Kiμ = 61 nM) and selectivity ( K i μ K i δ = 31 ).
Yoshio Okada - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of Stereoisomeric Analogues of Endomorphin-2, H-Tyr-Pro-Phe-Phe-NH2, and Examination of Their Opioid Receptor Binding Activities and Solution Conformation
Biochemical and biophysical research communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH(2)) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar mu- and delta-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d-amino acid isomers exhibited lower interaction with mu-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l-configuration was the most suitable for Binding within the mu Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for mu-Receptor-Binding sites.
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synthesis of stereoisomeric analogues of endomorphin 2 h tyr pro phe phe nh2 and examination of their opioid Receptor Binding activities and solution conformation
Biochemical and Biophysical Research Communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:Abstract All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar μ- and δ-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d -amino acid isomers exhibited lower interaction with μ-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l -configuration was the most suitable for Binding within the μ Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for μ-Receptor-Binding sites.
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amino acids and peptides lvi synthesis of pyrazinone ring containing opioid mimetics and examination of their opioid Receptor Binding Activity
Tetrahedron, 1999Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Junpei Yamazaki, Lawrence H. LazarusAbstract:Abstract Cyclization of dipeptidyl chloromethyl ketones gave 6-(4-aminobutyl)-3-carboxyethyl-5-methyl-2(1H)-pyrazinone (3), 3-(4-aminobutyl)-6-carboxyethyl-5-methyl-2(1H)-pyrazinone (6), and 3,6-bis(4-aminobutyl)-5-methyl-2(1H)-pyrazinone (15). Using above pyrazinone derivatives, three opioid mimetics were prepared (III-V). Derivatives containing 3 and 6 demonstrated weak μ and δ-opioid Receptor affinities ranging from 1.6 mM to 4.1 mM while the opioid mimetic containing derivative 15 displayed higher μ-opioid Receptor Binding affinity (Kiμ = 61 nM) and selectivity ( K i μ K i δ = 31 ).
Motohiro Takahashi - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of Stereoisomeric Analogues of Endomorphin-2, H-Tyr-Pro-Phe-Phe-NH2, and Examination of Their Opioid Receptor Binding Activities and Solution Conformation
Biochemical and biophysical research communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH(2)) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar mu- and delta-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d-amino acid isomers exhibited lower interaction with mu-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l-configuration was the most suitable for Binding within the mu Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for mu-Receptor-Binding sites.
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synthesis of stereoisomeric analogues of endomorphin 2 h tyr pro phe phe nh2 and examination of their opioid Receptor Binding activities and solution conformation
Biochemical and Biophysical Research Communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:Abstract All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar μ- and δ-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d -amino acid isomers exhibited lower interaction with μ-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l -configuration was the most suitable for Binding within the μ Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for μ-Receptor-Binding sites.
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amino acids and peptides lvi synthesis of pyrazinone ring containing opioid mimetics and examination of their opioid Receptor Binding Activity
Tetrahedron, 1999Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Junpei Yamazaki, Lawrence H. LazarusAbstract:Abstract Cyclization of dipeptidyl chloromethyl ketones gave 6-(4-aminobutyl)-3-carboxyethyl-5-methyl-2(1H)-pyrazinone (3), 3-(4-aminobutyl)-6-carboxyethyl-5-methyl-2(1H)-pyrazinone (6), and 3,6-bis(4-aminobutyl)-5-methyl-2(1H)-pyrazinone (15). Using above pyrazinone derivatives, three opioid mimetics were prepared (III-V). Derivatives containing 3 and 6 demonstrated weak μ and δ-opioid Receptor affinities ranging from 1.6 mM to 4.1 mM while the opioid mimetic containing derivative 15 displayed higher μ-opioid Receptor Binding affinity (Kiμ = 61 nM) and selectivity ( K i μ K i δ = 31 ).
Atsuko Fukumizu - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of Stereoisomeric Analogues of Endomorphin-2, H-Tyr-Pro-Phe-Phe-NH2, and Examination of Their Opioid Receptor Binding Activities and Solution Conformation
Biochemical and biophysical research communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH(2)) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar mu- and delta-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d-amino acid isomers exhibited lower interaction with mu-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l-configuration was the most suitable for Binding within the mu Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for mu-Receptor-Binding sites.
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synthesis of stereoisomeric analogues of endomorphin 2 h tyr pro phe phe nh2 and examination of their opioid Receptor Binding activities and solution conformation
Biochemical and Biophysical Research Communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:Abstract All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar μ- and δ-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d -amino acid isomers exhibited lower interaction with μ-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l -configuration was the most suitable for Binding within the μ Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for μ-Receptor-Binding sites.
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amino acids and peptides lvi synthesis of pyrazinone ring containing opioid mimetics and examination of their opioid Receptor Binding Activity
Tetrahedron, 1999Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Junpei Yamazaki, Lawrence H. LazarusAbstract:Abstract Cyclization of dipeptidyl chloromethyl ketones gave 6-(4-aminobutyl)-3-carboxyethyl-5-methyl-2(1H)-pyrazinone (3), 3-(4-aminobutyl)-6-carboxyethyl-5-methyl-2(1H)-pyrazinone (6), and 3,6-bis(4-aminobutyl)-5-methyl-2(1H)-pyrazinone (15). Using above pyrazinone derivatives, three opioid mimetics were prepared (III-V). Derivatives containing 3 and 6 demonstrated weak μ and δ-opioid Receptor affinities ranging from 1.6 mM to 4.1 mM while the opioid mimetic containing derivative 15 displayed higher μ-opioid Receptor Binding affinity (Kiμ = 61 nM) and selectivity ( K i μ K i δ = 31 ).
Toshio Yokoi - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of Stereoisomeric Analogues of Endomorphin-2, H-Tyr-Pro-Phe-Phe-NH2, and Examination of Their Opioid Receptor Binding Activities and Solution Conformation
Biochemical and biophysical research communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH(2)) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar mu- and delta-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d-amino acid isomers exhibited lower interaction with mu-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l-configuration was the most suitable for Binding within the mu Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for mu-Receptor-Binding sites.
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synthesis of stereoisomeric analogues of endomorphin 2 h tyr pro phe phe nh2 and examination of their opioid Receptor Binding activities and solution conformation
Biochemical and Biophysical Research Communications, 2000Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yoshiro Shimizu, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Lawrence H. LazarusAbstract:Abstract All sixteen stereoisomeric analogues of endomorphin-2 (H-Tyr-Pro-Phe-Phe-NH2) were synthesized by Fmoc-strategy using solid phase methods. Although synthetic endomorphin-2 exhibited similar μ- and δ-opioid Receptor-Binding Activity to the natural compound, endomorphin-2 analogues containing d -amino acid isomers exhibited lower interaction with μ-Receptors depending on the particular combination. The data clearly indicated that the three dimensional structure of endomorphin-2 with the natural l -configuration was the most suitable for Binding within the μ Receptor, but specific residues are important for Activity. Circular dichroism studies verified that changes in chirality of amino acids in the endomorphin-2 sequence resulted in structural conformation. These alterations significantly reduced the specificity for μ-Receptor-Binding sites.
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amino acids and peptides lvi synthesis of pyrazinone ring containing opioid mimetics and examination of their opioid Receptor Binding Activity
Tetrahedron, 1999Co-Authors: Yoshio Okada, Atsuko Fukumizu, Motohiro Takahashi, Yuko Tsuda, Toshio Yokoi, Sharon D. Bryant, Junpei Yamazaki, Lawrence H. LazarusAbstract:Abstract Cyclization of dipeptidyl chloromethyl ketones gave 6-(4-aminobutyl)-3-carboxyethyl-5-methyl-2(1H)-pyrazinone (3), 3-(4-aminobutyl)-6-carboxyethyl-5-methyl-2(1H)-pyrazinone (6), and 3,6-bis(4-aminobutyl)-5-methyl-2(1H)-pyrazinone (15). Using above pyrazinone derivatives, three opioid mimetics were prepared (III-V). Derivatives containing 3 and 6 demonstrated weak μ and δ-opioid Receptor affinities ranging from 1.6 mM to 4.1 mM while the opioid mimetic containing derivative 15 displayed higher μ-opioid Receptor Binding affinity (Kiμ = 61 nM) and selectivity ( K i μ K i δ = 31 ).
