A molecular dynamics study on opioid activities of biphalin molecule
Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hsieh, Jin-Yuan [verfasserIn] Chiang, Tzen-Yuh [verfasserIn] Chen, Jun-Liang [verfasserIn] Chen, Yun-Wen [verfasserIn] Lin, Hong-Chang [verfasserIn] Hwang, Chi-Chuan [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2010 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of molecular modeling - Berlin : Springer, 1995, 17(2010), 10 vom: 23. Dez., Seite 2455-2464 |
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| Übergeordnetes Werk: |
volume:17 ; year:2010 ; number:10 ; day:23 ; month:12 ; pages:2455-2464 |
| Links: |
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| DOI / URN: |
10.1007/s00894-010-0931-1 |
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| Katalog-ID: |
SPR007889968 |
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| 100 | 1 | |a Hsieh, Jin-Yuan |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A molecular dynamics study on opioid activities of biphalin molecule |
| 264 | 1 | |c 2010 | |
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| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 520 | |a Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. | ||
| 650 | 4 | |a Biphalin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Molecular dynamics |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Opioid activities |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Chiang, Tzen-Yuh |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Jun-Liang |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Yun-Wen |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Hong-Chang |e verfasserin |4 aut | |
| 700 | 1 | |a Hwang, Chi-Chuan |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of molecular modeling |d Berlin : Springer, 1995 |g 17(2010), 10 vom: 23. Dez., Seite 2455-2464 |w (DE-627)188861203 |w (DE-600)1284729-X |x 0948-5023 |7 nnns |
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| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00894-010-0931-1 |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2070 | ||
| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
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| 912 | |a GBV_ILN_2106 | ||
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| 912 | |a GBV_ILN_2110 | ||
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| 912 | |a GBV_ILN_2116 | ||
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2010 |
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35.00 44.42 |
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| allfields |
10.1007/s00894-010-0931-1 doi (DE-627)SPR007889968 (SPR)s00894-010-0931-1-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl 44.42 bkl Hsieh, Jin-Yuan verfasserin aut A molecular dynamics study on opioid activities of biphalin molecule 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 Chiang, Tzen-Yuh verfasserin aut Chen, Jun-Liang verfasserin aut Chen, Yun-Wen verfasserin aut Lin, Hong-Chang verfasserin aut Hwang, Chi-Chuan verfasserin aut Enthalten in Journal of molecular modeling Berlin : Springer, 1995 17(2010), 10 vom: 23. Dez., Seite 2455-2464 (DE-627)188861203 (DE-600)1284729-X 0948-5023 nnns volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 https://dx.doi.org/10.1007/s00894-010-0931-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA SSG-OPC-PHA SSG-OPC-ASE GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 44.42 ASE AR 17 2010 10 23 12 2455-2464 |
| spelling |
10.1007/s00894-010-0931-1 doi (DE-627)SPR007889968 (SPR)s00894-010-0931-1-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl 44.42 bkl Hsieh, Jin-Yuan verfasserin aut A molecular dynamics study on opioid activities of biphalin molecule 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 Chiang, Tzen-Yuh verfasserin aut Chen, Jun-Liang verfasserin aut Chen, Yun-Wen verfasserin aut Lin, Hong-Chang verfasserin aut Hwang, Chi-Chuan verfasserin aut Enthalten in Journal of molecular modeling Berlin : Springer, 1995 17(2010), 10 vom: 23. Dez., Seite 2455-2464 (DE-627)188861203 (DE-600)1284729-X 0948-5023 nnns volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 https://dx.doi.org/10.1007/s00894-010-0931-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA SSG-OPC-PHA SSG-OPC-ASE GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 44.42 ASE AR 17 2010 10 23 12 2455-2464 |
| allfields_unstemmed |
10.1007/s00894-010-0931-1 doi (DE-627)SPR007889968 (SPR)s00894-010-0931-1-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl 44.42 bkl Hsieh, Jin-Yuan verfasserin aut A molecular dynamics study on opioid activities of biphalin molecule 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 Chiang, Tzen-Yuh verfasserin aut Chen, Jun-Liang verfasserin aut Chen, Yun-Wen verfasserin aut Lin, Hong-Chang verfasserin aut Hwang, Chi-Chuan verfasserin aut Enthalten in Journal of molecular modeling Berlin : Springer, 1995 17(2010), 10 vom: 23. Dez., Seite 2455-2464 (DE-627)188861203 (DE-600)1284729-X 0948-5023 nnns volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 https://dx.doi.org/10.1007/s00894-010-0931-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA SSG-OPC-PHA SSG-OPC-ASE GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 44.42 ASE AR 17 2010 10 23 12 2455-2464 |
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10.1007/s00894-010-0931-1 doi (DE-627)SPR007889968 (SPR)s00894-010-0931-1-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl 44.42 bkl Hsieh, Jin-Yuan verfasserin aut A molecular dynamics study on opioid activities of biphalin molecule 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 Chiang, Tzen-Yuh verfasserin aut Chen, Jun-Liang verfasserin aut Chen, Yun-Wen verfasserin aut Lin, Hong-Chang verfasserin aut Hwang, Chi-Chuan verfasserin aut Enthalten in Journal of molecular modeling Berlin : Springer, 1995 17(2010), 10 vom: 23. Dez., Seite 2455-2464 (DE-627)188861203 (DE-600)1284729-X 0948-5023 nnns volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 https://dx.doi.org/10.1007/s00894-010-0931-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA SSG-OPC-PHA SSG-OPC-ASE GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 44.42 ASE AR 17 2010 10 23 12 2455-2464 |
| allfieldsSound |
10.1007/s00894-010-0931-1 doi (DE-627)SPR007889968 (SPR)s00894-010-0931-1-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl 44.42 bkl Hsieh, Jin-Yuan verfasserin aut A molecular dynamics study on opioid activities of biphalin molecule 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 Chiang, Tzen-Yuh verfasserin aut Chen, Jun-Liang verfasserin aut Chen, Yun-Wen verfasserin aut Lin, Hong-Chang verfasserin aut Hwang, Chi-Chuan verfasserin aut Enthalten in Journal of molecular modeling Berlin : Springer, 1995 17(2010), 10 vom: 23. Dez., Seite 2455-2464 (DE-627)188861203 (DE-600)1284729-X 0948-5023 nnns volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 https://dx.doi.org/10.1007/s00894-010-0931-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA SSG-OPC-PHA SSG-OPC-ASE GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 44.42 ASE AR 17 2010 10 23 12 2455-2464 |
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English |
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Enthalten in Journal of molecular modeling 17(2010), 10 vom: 23. Dez., Seite 2455-2464 volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 |
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Enthalten in Journal of molecular modeling 17(2010), 10 vom: 23. Dez., Seite 2455-2464 volume:17 year:2010 number:10 day:23 month:12 pages:2455-2464 |
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Biphalin Molecular dynamics Opioid activities |
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Hsieh, Jin-Yuan @@aut@@ Chiang, Tzen-Yuh @@aut@@ Chen, Jun-Liang @@aut@@ Chen, Yun-Wen @@aut@@ Lin, Hong-Chang @@aut@@ Hwang, Chi-Chuan @@aut@@ |
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2010-12-23T00:00:00Z |
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|
| author |
Hsieh, Jin-Yuan |
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Hsieh, Jin-Yuan ddc 540 bkl 35.00 bkl 44.42 misc Biphalin misc Molecular dynamics misc Opioid activities A molecular dynamics study on opioid activities of biphalin molecule |
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540 ASE 35.00 bkl 44.42 bkl A molecular dynamics study on opioid activities of biphalin molecule Biphalin (dpeaa)DE-He213 Molecular dynamics (dpeaa)DE-He213 Opioid activities (dpeaa)DE-He213 |
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ddc 540 bkl 35.00 bkl 44.42 misc Biphalin misc Molecular dynamics misc Opioid activities |
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ddc 540 bkl 35.00 bkl 44.42 misc Biphalin misc Molecular dynamics misc Opioid activities |
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ddc 540 bkl 35.00 bkl 44.42 misc Biphalin misc Molecular dynamics misc Opioid activities |
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A molecular dynamics study on opioid activities of biphalin molecule |
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Hsieh, Jin-Yuan |
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Hsieh, Jin-Yuan Chiang, Tzen-Yuh Chen, Jun-Liang Chen, Yun-Wen Lin, Hong-Chang Hwang, Chi-Chuan |
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Hsieh, Jin-Yuan |
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10.1007/s00894-010-0931-1 |
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verfasserin |
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molecular dynamics study on opioid activities of biphalin molecule |
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A molecular dynamics study on opioid activities of biphalin molecule |
| abstract |
Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. |
| abstractGer |
Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. |
| abstract_unstemmed |
Abstract Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH)2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-$ NH_{2} $ were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges %$ {\hbox{C}}_4^{\alpha } - {{\hbox{C}}_4}\prime - {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} %$ and %$ {{\hbox{N}}_9} - {{\hbox{N}}_{{10}}} - {{\hbox{C}}_5}\prime - {\hbox{C}}_5^{\alpha } %$, which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle $ χ^{2} $ at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe. |
| collection_details |
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| container_issue |
10 |
| title_short |
A molecular dynamics study on opioid activities of biphalin molecule |
| url |
https://dx.doi.org/10.1007/s00894-010-0931-1 |
| remote_bool |
true |
| author2 |
Chiang, Tzen-Yuh Chen, Jun-Liang Chen, Yun-Wen Lin, Hong-Chang Hwang, Chi-Chuan |
| author2Str |
Chiang, Tzen-Yuh Chen, Jun-Liang Chen, Yun-Wen Lin, Hong-Chang Hwang, Chi-Chuan |
| ppnlink |
188861203 |
| mediatype_str_mv |
c |
| isOA_txt |
false |
| hochschulschrift_bool |
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| doi_str |
10.1007/s00894-010-0931-1 |
| up_date |
2024-07-03T15:55:02.555Z |
| _version_ |
1803573896211857408 |
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| score |
7.4014616 |