Characterization of ICAM-1 biophore to design cytoadherence blocking peptides
Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model re...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mehra, A [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. |
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| Schlagwörter: |
Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism |
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| Übergeordnetes Werk: |
Enthalten in: Journal of molecular graphics and modelling - New York, NY : Elsevier, 1997, 57(2015), Seite 27-35 |
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| Übergeordnetes Werk: |
volume:57 ; year:2015 ; pages:27-35 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jmgm.2015.01.004 |
|---|
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| 520 | |a Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. | ||
| 540 | |a Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. | ||
| 650 | 4 | |a Peptides - immunology | |
| 650 | 4 | |a Peptides - chemical synthesis | |
| 650 | 4 | |a Intercellular Adhesion Molecule-1 - chemistry | |
| 650 | 4 | |a Protein Binding - drug effects | |
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10.1016/j.jmgm.2015.01.004 doi PQ20160617 (DE-627)OLC1956588477 (DE-599)GBVOLC1956588477 (PRQ)c1554-8565186b8bf507631b8d406f42622e7c0c4279d3bd23b9c694aa85e9d1563ec0 (KEY)0123094820150000057000000027characterizationoficam1biophoretodesigncytoadheren DE-627 ger DE-627 rakwb eng 540 004 DNB Mehra, A verfasserin aut Characterization of ICAM-1 biophore to design cytoadherence blocking peptides 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. Peptides - immunology Peptides - chemical synthesis Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism Peptides - pharmacology Plasmodium falciparum - metabolism Peptides - chemistry Cell Adhesion - drug effects Jerath, Gaurav oth Ramakrishnan, Vibin oth Trivedi, Vishal oth Enthalten in Journal of molecular graphics and modelling New York, NY : Elsevier, 1997 57(2015), Seite 27-35 (DE-627)234649232 (DE-600)1396450-1 (DE-576)062210920 1093-3263 nnns volume:57 year:2015 pages:27-35 http://dx.doi.org/10.1016/j.jmgm.2015.01.004 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25625914 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 57 2015 27-35 |
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10.1016/j.jmgm.2015.01.004 doi PQ20160617 (DE-627)OLC1956588477 (DE-599)GBVOLC1956588477 (PRQ)c1554-8565186b8bf507631b8d406f42622e7c0c4279d3bd23b9c694aa85e9d1563ec0 (KEY)0123094820150000057000000027characterizationoficam1biophoretodesigncytoadheren DE-627 ger DE-627 rakwb eng 540 004 DNB Mehra, A verfasserin aut Characterization of ICAM-1 biophore to design cytoadherence blocking peptides 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. Peptides - immunology Peptides - chemical synthesis Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism Peptides - pharmacology Plasmodium falciparum - metabolism Peptides - chemistry Cell Adhesion - drug effects Jerath, Gaurav oth Ramakrishnan, Vibin oth Trivedi, Vishal oth Enthalten in Journal of molecular graphics and modelling New York, NY : Elsevier, 1997 57(2015), Seite 27-35 (DE-627)234649232 (DE-600)1396450-1 (DE-576)062210920 1093-3263 nnns volume:57 year:2015 pages:27-35 http://dx.doi.org/10.1016/j.jmgm.2015.01.004 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25625914 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 57 2015 27-35 |
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10.1016/j.jmgm.2015.01.004 doi PQ20160617 (DE-627)OLC1956588477 (DE-599)GBVOLC1956588477 (PRQ)c1554-8565186b8bf507631b8d406f42622e7c0c4279d3bd23b9c694aa85e9d1563ec0 (KEY)0123094820150000057000000027characterizationoficam1biophoretodesigncytoadheren DE-627 ger DE-627 rakwb eng 540 004 DNB Mehra, A verfasserin aut Characterization of ICAM-1 biophore to design cytoadherence blocking peptides 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. Peptides - immunology Peptides - chemical synthesis Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism Peptides - pharmacology Plasmodium falciparum - metabolism Peptides - chemistry Cell Adhesion - drug effects Jerath, Gaurav oth Ramakrishnan, Vibin oth Trivedi, Vishal oth Enthalten in Journal of molecular graphics and modelling New York, NY : Elsevier, 1997 57(2015), Seite 27-35 (DE-627)234649232 (DE-600)1396450-1 (DE-576)062210920 1093-3263 nnns volume:57 year:2015 pages:27-35 http://dx.doi.org/10.1016/j.jmgm.2015.01.004 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25625914 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 57 2015 27-35 |
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10.1016/j.jmgm.2015.01.004 doi PQ20160617 (DE-627)OLC1956588477 (DE-599)GBVOLC1956588477 (PRQ)c1554-8565186b8bf507631b8d406f42622e7c0c4279d3bd23b9c694aa85e9d1563ec0 (KEY)0123094820150000057000000027characterizationoficam1biophoretodesigncytoadheren DE-627 ger DE-627 rakwb eng 540 004 DNB Mehra, A verfasserin aut Characterization of ICAM-1 biophore to design cytoadherence blocking peptides 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. Peptides - immunology Peptides - chemical synthesis Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism Peptides - pharmacology Plasmodium falciparum - metabolism Peptides - chemistry Cell Adhesion - drug effects Jerath, Gaurav oth Ramakrishnan, Vibin oth Trivedi, Vishal oth Enthalten in Journal of molecular graphics and modelling New York, NY : Elsevier, 1997 57(2015), Seite 27-35 (DE-627)234649232 (DE-600)1396450-1 (DE-576)062210920 1093-3263 nnns volume:57 year:2015 pages:27-35 http://dx.doi.org/10.1016/j.jmgm.2015.01.004 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25625914 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 57 2015 27-35 |
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10.1016/j.jmgm.2015.01.004 doi PQ20160617 (DE-627)OLC1956588477 (DE-599)GBVOLC1956588477 (PRQ)c1554-8565186b8bf507631b8d406f42622e7c0c4279d3bd23b9c694aa85e9d1563ec0 (KEY)0123094820150000057000000027characterizationoficam1biophoretodesigncytoadheren DE-627 ger DE-627 rakwb eng 540 004 DNB Mehra, A verfasserin aut Characterization of ICAM-1 biophore to design cytoadherence blocking peptides 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. Nutzungsrecht: Copyright © 2015 Elsevier Inc. All rights reserved. Peptides - immunology Peptides - chemical synthesis Intercellular Adhesion Molecule-1 - chemistry Protein Binding - drug effects Protozoan Proteins - chemistry Protozoan Proteins - metabolism Peptides - pharmacology Plasmodium falciparum - metabolism Peptides - chemistry Cell Adhesion - drug effects Jerath, Gaurav oth Ramakrishnan, Vibin oth Trivedi, Vishal oth Enthalten in Journal of molecular graphics and modelling New York, NY : Elsevier, 1997 57(2015), Seite 27-35 (DE-627)234649232 (DE-600)1396450-1 (DE-576)062210920 1093-3263 nnns volume:57 year:2015 pages:27-35 http://dx.doi.org/10.1016/j.jmgm.2015.01.004 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25625914 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 57 2015 27-35 |
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Characterization of ICAM-1 biophore to design cytoadherence blocking peptides |
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Characterization of ICAM-1 biophore to design cytoadherence blocking peptides |
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characterization of icam-1 biophore to design cytoadherence blocking peptides |
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Characterization of ICAM-1 biophore to design cytoadherence blocking peptides |
| abstract |
Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. |
| abstractGer |
Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. |
| abstract_unstemmed |
Peptides from natural sources are good starting material to design bioactive agents with desired therapeutic property. IB peptide derived from the ICAM-1 has been studied extensively as an agent to disrupt the non-specific binding of lymphocyte to the endothelial cells. ICAM-1: IB molecular model reveals that IB peptide binds in an extended conformation to the ICAM-1, masking LFA-1 and partially covering PfEMP-1 binding site. Considering the regioselective requirement of ICAM-1: PfEMP1 binding site, IB peptide charge and 3-D conformation are optimized through generation of combinatorial peptide library containing single, double, triple, tetra and quadra amino acid substitutions of IB peptide. Further, truncation of IB peptide followed by molecular modeling studies gave us the biophoric environment of the IB peptide required for its activity. Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding. Molecular dynamics simulations were performed for 10ns each under four different temperatures to estimate comparative stability of ICAM1: IB peptide complexes. The designed peptide ICAM1: IBT213 has comparable stability at ambient temperature, while ICAM1: IBT1 shows a greater degree of robustness at higher temperatures. Overall, the study has given useful insights into IB peptide binding site on ICAM1 and its potential in designing novel peptides to disrupt the cytoadherence complex involving ICAM1: PfEMP1. |
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Characterization of ICAM-1 biophore to design cytoadherence blocking peptides |
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http://dx.doi.org/10.1016/j.jmgm.2015.01.004 http://www.ncbi.nlm.nih.gov/pubmed/25625914 |
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