The Experts below are selected from a list of 225 Experts worldwide ranked by ideXlab platform
Horst Kessler - One of the best experts on this subject based on the ideXlab platform.
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arg gly asp constrained within cyclic pentapoptides strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment p1
FEBS Letters, 1991Co-Authors: Monique Aumailley, Marion Gurrath, Gerhard Muller, Juan J Calvete, Rupert Timpl, Horst KesslerAbstract:Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.
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Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
FEBS Letters, 1991Co-Authors: Monique Aumailley, Marion Gurrath, Gerhard Muller, Juan J Calvete, Rupert Timpl, Horst KesslerAbstract:Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.
John Marshall - One of the best experts on this subject based on the ideXlab platform.
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Structure-function analysis of arg-Gly-Asp helix motifs in αvβ6 inteqrin liqands
Journal of Biological Chemistry, 2020Co-Authors: Danielle Dicara, Chiara Rapisarda, Julie L. Sutcliffe, Shelia M. Violette, Paul H. Weinreb, Ian R. Hart, Mark J. Howard, John MarshallAbstract:Data relating to the structural basis of ligand recognition by integrins are limited. Here we describe the physical requirements for high affinity binding of ligands to αvβ6. By combining a series of structural analyses with functional testing, we show that 20-mer peptide ligands, derived from high affinity ligands of αvβ6 (foot-and-mouth-disease virus, latency associated peptide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed immediately by a C-terminal helix. This arrangement allows two conserved Leu/ lie residues at Asp +1 and Asp +4 to be presented on the outside face of the helix enabling a potential hydrophobic interaction with the αcvβ6 integrin, in addition to the Arg-Gly-Asp interaction. The extent of the helix determines peptide affinity for αvβ6 and potency as an αvβ6 antagonist. A major role of this C-terminal helix is likely to be the correct positioning of the Asp +1 and Asp +4 residues. These data suggest an explanation for several biological functions of αvβ6 and provide a structural platform for design of αvβ6 antagonists.
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structure function analysis of arg gly asp helix motifs in alpha v beta 6 integrin ligands
Journal of Biological Chemistry, 2007Co-Authors: Danielle Dicara, Chiara Rapisarda, Julie L. Sutcliffe, Shelia M. Violette, Paul H. Weinreb, Ian R. Hart, Mark J. Howard, John MarshallAbstract:Data relating to the structural basis of ligand recognition by integrins are limited. Here we describe the physical requirements for high affinity binding of ligands to alpha v beta 6. By combining a series of structural analyses with functional testing, we show that 20-mer peptide ligands, derived from high affinity ligands of alpha v beta 6 (foot-and-mouth-disease virus, latency associated peptide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed immediately by a C-terminal helix. This arrangement allows two conserved Leu/Ile residues at Asp(+1) and Asp(+4) to be presented on the outside face of the helix enabling a potential hydrophobic interaction with the alpha v beta 6 integrin, in addition to the Arg-Gly-Asp interaction. The extent of the helix determines peptide affinity for alpha v beta 6 and potency as an alpha v beta 6 antagonist. A major role of this C-terminal helix is likely to be the correct positioning of the Asp(+1) and Asp(+4) residues. These data suggest an explanation for several biological functions of alpha v beta 6 and provide a structural platform for design of alpha v beta 6 antagonists.
Monique Aumailley - One of the best experts on this subject based on the ideXlab platform.
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arg gly asp constrained within cyclic pentapoptides strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment p1
FEBS Letters, 1991Co-Authors: Monique Aumailley, Marion Gurrath, Gerhard Muller, Juan J Calvete, Rupert Timpl, Horst KesslerAbstract:Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.
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Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
FEBS Letters, 1991Co-Authors: Monique Aumailley, Marion Gurrath, Gerhard Muller, Juan J Calvete, Rupert Timpl, Horst KesslerAbstract:Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.
Danielle Dicara - One of the best experts on this subject based on the ideXlab platform.
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Structure-function analysis of arg-Gly-Asp helix motifs in αvβ6 inteqrin liqands
Journal of Biological Chemistry, 2020Co-Authors: Danielle Dicara, Chiara Rapisarda, Julie L. Sutcliffe, Shelia M. Violette, Paul H. Weinreb, Ian R. Hart, Mark J. Howard, John MarshallAbstract:Data relating to the structural basis of ligand recognition by integrins are limited. Here we describe the physical requirements for high affinity binding of ligands to αvβ6. By combining a series of structural analyses with functional testing, we show that 20-mer peptide ligands, derived from high affinity ligands of αvβ6 (foot-and-mouth-disease virus, latency associated peptide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed immediately by a C-terminal helix. This arrangement allows two conserved Leu/ lie residues at Asp +1 and Asp +4 to be presented on the outside face of the helix enabling a potential hydrophobic interaction with the αcvβ6 integrin, in addition to the Arg-Gly-Asp interaction. The extent of the helix determines peptide affinity for αvβ6 and potency as an αvβ6 antagonist. A major role of this C-terminal helix is likely to be the correct positioning of the Asp +1 and Asp +4 residues. These data suggest an explanation for several biological functions of αvβ6 and provide a structural platform for design of αvβ6 antagonists.
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structure function analysis of arg gly asp helix motifs in alpha v beta 6 integrin ligands
Journal of Biological Chemistry, 2007Co-Authors: Danielle Dicara, Chiara Rapisarda, Julie L. Sutcliffe, Shelia M. Violette, Paul H. Weinreb, Ian R. Hart, Mark J. Howard, John MarshallAbstract:Data relating to the structural basis of ligand recognition by integrins are limited. Here we describe the physical requirements for high affinity binding of ligands to alpha v beta 6. By combining a series of structural analyses with functional testing, we show that 20-mer peptide ligands, derived from high affinity ligands of alpha v beta 6 (foot-and-mouth-disease virus, latency associated peptide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed immediately by a C-terminal helix. This arrangement allows two conserved Leu/Ile residues at Asp(+1) and Asp(+4) to be presented on the outside face of the helix enabling a potential hydrophobic interaction with the alpha v beta 6 integrin, in addition to the Arg-Gly-Asp interaction. The extent of the helix determines peptide affinity for alpha v beta 6 and potency as an alpha v beta 6 antagonist. A major role of this C-terminal helix is likely to be the correct positioning of the Asp(+1) and Asp(+4) residues. These data suggest an explanation for several biological functions of alpha v beta 6 and provide a structural platform for design of alpha v beta 6 antagonists.
Klaus Biemann - One of the best experts on this subject based on the ideXlab platform.
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amino acid sequence of a protease inhibitor isolated from sarcophaga bullata determined by mass spectrometry
Protein Science, 2008Co-Authors: Ioannis A Papayannopoulos, Klaus BiemannAbstract:The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.
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Amino acid sequence of a protease inhibitor isolated from Sarcophaga bullata determined w
1992Co-Authors: Klaus BiemannAbstract:The amino acid sequence of a protease inhibitor isolated from the hemolymph of Sarcophaga bullata larvae was determined by tandem mass spectrometry. Homology considerations with respect to other protease inhibitors with known primary structures assisted in the choice of the procedure followed in the sequence determination and in the alignment of the various peptides obtained from specific chemical cleavage at cysteines and enzyme digests of the S. bullata protease inhibitor. The resulting sequence of 57 residues is as follows: Val Asp Lys Ser Ala Cys Leu Gln Pro Lys Glu Val Gly Pro Cys Arg Lys Ser Asp Phe Val Phe Phe Tyr Asn Ala Asp Thr Lys Ala Cys Glu Glu Phe Leu Tyr Gly Gly Cys Arg Gly Asn Asp Asn Arg Phe Asn Thr Lys Glu Glu Cys Glu Lys Leu Cys Leu.