The Experts below are selected from a list of 204 Experts worldwide ranked by ideXlab platform
Claudio Toniolo - One of the best experts on this subject based on the ideXlab platform.
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slow tert butyl ester acidolysis and peptide 310 helix to α helix transition in hfip solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Slow tert‐butyl ester acidolysis and peptide 310‐helix to α‐helix transition in HFIP solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Françoise Fauvel-lafève - One of the best experts on this subject based on the ideXlab platform.
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A new platelet receptor specific to type III collagen. Type III collagen-binding protein.
The Journal of biological chemistry, 2000Co-Authors: Emmanuel Monnet, Françoise Fauvel-lafèveAbstract:Abstract Platelet interaction with type III collagen is mediated by several platelet receptors that recognize specific sequences in collagen. We previously described an Octapeptide KP*GEP*GPK within the α(1)III-CB4 fragment that binds to platelets and specifically inhibits platelet aggregation induced by type III collagen. In this study, we demonstrated that the Octapeptide prevented platelet contact and spreading on type III collagen and subendothelium under static and flow conditions. Platelets adhered to the immobilized Octapeptide, and anti-bodies directed against other platelet collagen receptors (glycoprotein (GP) Ia/IIa, GP IV, p65, p47) did not impair this adhesion. The platelet Octapeptide receptor was identified by ligand blotting as a protein doublet with molecular masses of 68 and 72 kDa and does not correspond to any other already known platelet collagen receptors (GP Ia, GP IV GP VI, and p65). Our results indicate that a specific type III collagen receptor, expressed on the platelet surface, is involved in the first stages of platelet type III collagen interaction.
Alessandro Moretto - One of the best experts on this subject based on the ideXlab platform.
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slow tert butyl ester acidolysis and peptide 310 helix to α helix transition in hfip solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Slow tert‐butyl ester acidolysis and peptide 310‐helix to α‐helix transition in HFIP solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Fernando Formaggio - One of the best experts on this subject based on the ideXlab platform.
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slow tert butyl ester acidolysis and peptide 310 helix to α helix transition in hfip solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Slow tert‐butyl ester acidolysis and peptide 310‐helix to α‐helix transition in HFIP solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Quirinus B. Broxterman - One of the best experts on this subject based on the ideXlab platform.
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slow tert butyl ester acidolysis and peptide 310 helix to α helix transition in hfip solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Slow tert‐butyl ester acidolysis and peptide 310‐helix to α‐helix transition in HFIP solution
Biopolymers, 2007Co-Authors: Alessandro Moretto, Quirinus B. Broxterman, Bernard Kaptein, Timothy A Keiderling, Fernando Formaggio, Marco Crisma, Claudio TonioloAbstract:We have already shown by CD and NMR techniques that the terminally protected homo-Octapeptides Z (and Ac)-[L-(αMe)Val]8-OtBu undergo a slow and irreversible 310-helix to α-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding Octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 233–238, 2007. This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
