[NMR paper] Synthesis, biological activity and NMR-based structural studies of deltorphin I analogues modified in message domain with a new ?,?-disubstituted glycines.
Synthesis, biological activity and NMR-based structural studies of deltorphin I analogues modified in message domain with a new ?,?-disubstituted glycines.
Related ArticlesSynthesis, biological activity and NMR-based structural studies of deltorphin I analogues modified in message domain with a new ?,?-disubstituted glycines.
Chem Biol Drug Des. 2016 Jan 25;
Authors: Lasota A, Fr?czak O, Muchowska A, Nowakowski M, Maciejczyk M, Ejchart A, Olma A
Abstract
This paper describes new deltorphin I analogues in which phenylalanine residues were replaced by the corresponding (R) or (S)-?-benzyl-?-azidoalanine, ?-benzyl-?-(1-pyrrolidinyl)alanine, ?-benzyl-?-(1-piperidinyl)alanine and ?-benzyl-?-(4-morpholinyl)-alanine residues. The potency and selectivity of the new analogues were evaluated by a competitive receptor binding assay in the rat brain using [(3) H]DAMGO (a ? ligand) and [(3) H]DELT (a ? ligand). The affinity of analogues containing (R) or (S)-?-benzyl-?-azidoalanine in position 3 to ?-receptors strongly depended on the chirality of the ?,?-disubstituted residue. The conformational behavior of peptides modified with (R) or (S)-?-benzyl-?-(1-piperidinyl)Ala, which display the opposite selectivity, was analyzed by (1) H and (13) C NMR. The ?-selective Tyr-D-Ala-(R)-?-benzyl-?-(1-piperidinyl)Ala-Asp-Val-Val-Gly-NH2 lacks the helical conformation observed in the ?-selective Tyr-D-Ala-(S)-?-benzyl-?-(1-piperidinyl)Ala-Asp-Val-Val-Gly-NH2 . Our results support the proposal that differences between ?- and ?-selective opioid peptides are attributable to the presence or absence of a spatial overlap between the N-terminal message domain and the C-terminal address domain. This article is protected by copyright. All rights reserved.
PMID: 26808639 [PubMed - as supplied by publisher]
[NMR paper] Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Related Articles Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Chembiochem. 2014 Nov 18;
Authors: Rauthu SR, Shiao TC, André S, Miller MC, Madej E, Mayo KH, Gabius HJ, Roy R
Abstract
The emerging significance of...
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[NMR paper] Synthesis, Biological Evaluation, WAC and NMR Studies of S-Galactosides and Non-Carbohydrate Ligands of Cholera Toxin Based on Polyhydroxyalkylfuroate Moieties.
Synthesis, Biological Evaluation, WAC and NMR Studies of S-Galactosides and Non-Carbohydrate Ligands of Cholera Toxin Based on Polyhydroxyalkylfuroate Moieties.
Related Articles Synthesis, Biological Evaluation, WAC and NMR Studies of S-Galactosides and Non-Carbohydrate Ligands of Cholera Toxin Based on Polyhydroxyalkylfuroate Moieties.
Chemistry. 2013 Nov 21;
Authors: Ramos-Soriano J, Niss U, Angulo J, Angulo M, Moreno-Vargas AJ, Carmona AT, Ohlson S, Robina I
Abstract
The synthesis of several non-carbohydrate ligands of cholera toxin...
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11-23-2013 05:08 PM
[NMR paper] Micelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
Micelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
Related Articles Micelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
J Biomol Struct Dyn. 2013;31(7):748-64
Authors: Sikorska E, Kwiatkowska A
Abstract
In this study, by applying a combined approach of NMR measurements and molecular modelling, the conformations and the interactions with membrane-like...
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[NMR paper] Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Org Biomol Chem. 2013 Jan 28;11(4):640-7
Authors: Sternberg U, Birtalan E, Jakovkin I, Luy B, Schepers U, Bräse S, Muhle-Goll C
Abstract
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Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Feb 1;17(5):1519-1528
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute...
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Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Jan 5;
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute 2 protein of...
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[NMR paper] NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similari
NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
Eur J Biochem. 1995 Nov 1;233(3):847-55
Authors: Polshakov VI, Frenkiel TA,...
Synthesis, biological activity and NMR-based structural studies of deltorphin I analogues modified in message domain with a new ?,?-disubstituted glycines.
Linear Mode
