[NMR paper] SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target.
SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target.
Related ArticlesSPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target.
J Pept Sci. 2020 Feb;26(2):e3231
Authors: De Luca S, Verdoliva V, Saviano M, Fattorusso R, Diana D
Abstract
The binding process of A9 peptide toward HER2-DIVMP, a synthetic model of the receptor domain IV, was studied by using the surface plasmon resonance (SPR) technique, with the aim of validating it as a fast and reliable screening method for selecting peptide ligands specifically targeting a domain of their target. To investigate the structural basis of A9 binding to the model of HER2-DIVMP, multiple ligand-based nuclear magnetic resonance (NMR) methods were applied. The use of saturation transfer difference (STD) and WaterLOGSY NMR experiments identified key residues in the peptide for the receptor binding. Moreover, the bound conformation of the A9 peptide was obtained using transferred nuclear Overhauser effect spectroscopy (trNOESY) experiments. The NMR data revealed an extended binding surface that confirms an in silico model previously reported. These structural findings could provide good starting points for future lead structures optimization specific for the receptor target.
[NMR paper] Using 1H and 13C NMR chemical shifts to determine cyclic peptide conformations: a combined molecular dynamics and quantum mechanics approach.
Using 1H and 13C NMR chemical shifts to determine cyclic peptide conformations: a combined molecular dynamics and quantum mechanics approach.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Using 1H and 13C NMR chemical shifts to determine cyclic peptide conformations: a combined molecular dynamics and quantum mechanics approach.
Phys Chem Chem Phys. 2018 May 23;20(20):14003-14012
Authors: Nguyen QNN, Schwochert J, Tantillo DJ, Lokey RS
Abstract
...
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06-01-2018 12:44 PM
[NMR paper] A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
ChemMedChem. 2017 Sep 07;12(17):1458-1463
Authors: Dalvit C, Santi S, Neier R
Abstract
Over the...
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09-24-2017 06:16 AM
[NMR paper] Probing the Interaction between cHAVc3 Peptide and the EC1 Domain of E-cadherin using NMR and Molecular Dynamics Simulations.
Probing the Interaction between cHAVc3 Peptide and the EC1 Domain of E-cadherin using NMR and Molecular Dynamics Simulations.
Related Articles Probing the Interaction between cHAVc3 Peptide and the EC1 Domain of E-cadherin using NMR and Molecular Dynamics Simulations.
J Biomol Struct Dyn. 2016 Jan 5;:1-48
Authors: Alaofi A, Farokhi E, Prasasty VD, Anbanandam A, Kuczera K, Siahaan TJ
Abstract
The goal of this work is to probe the interaction between cyclic cHAVc3 peptide and the EC1 domain of human E-cadherin protein. Cyclic...
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01-07-2016 08:36 AM
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
Chem Commun (Camb). 2011 Jun 14;47(22):6407-9
Authors: Shoshan MS, Shalev DE, Adriaens W, Merkx M, Hackeng TM, Tshuva EY
Abstract
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ~3.0 and ~6.8 Cu(I) binds through one Cys and the Met...
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09-21-2011 03:31 PM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
J Med Chem. 2011 Jan 27;
Authors: Orcajo-Rinco?n AL, Ortega-Gutie?rrez S, Serrano P, Torrecillas IR, Wu?thrich K, Campillo M, Pardo L, Viso A, Benhamu? B, Lo?pez-Rodri?guez ML
We report a novel series of non-peptide ligands that inhibit the growth...
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01-29-2011 12:35 PM
[NMR paper] Design, NMR characterization and activity of a 21-residue peptide fragment of bacteri
Design, NMR characterization and activity of a 21-residue peptide fragment of bacteriocin AS-48 containing its putative membrane interacting region.
Related Articles Design, NMR characterization and activity of a 21-residue peptide fragment of bacteriocin AS-48 containing its putative membrane interacting region.
J Pept Sci. 2005 Jan;11(1):29-36
Authors: Jiménez MA, Barrachi-Saccilotto AC, Valdivia E, Maqueda M, Rico M
Bacteriocin AS-48 is a 70-residue cyclic polypeptide from Enterococcus faecalis that shows a broad antimicrobial spectrum...
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11-24-2010 11:14 PM
[NMR paper] Structural characterization of peptide hormone/receptor interactions by NMR spectrosc
Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
Biopolymers. 1999;51(3):208-20
Authors: Pellegrini M, Mierke DF
The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled...
SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target.
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