Related ArticlesRole of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
J Dent. 2014 Jan 16;
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagam J
Abstract
Objections: Functional adhesive monomers are formulated with solvents and hydrophilic resin monomers, such as 2-hydroxyethyl methacrylate (HEMA). In theory, exposed collagen fibrils should be covered and protected by the resin matrix. We examined if the atomic- and molecular-level interaction of monomers with collagen would be affected when the monomers are blended with HEMA. Methods: We performed saturation transfer difference (STD) NMR spectroscopy to investigate the binding interaction of two functional monomers, 4-methacryloyloxyethyl trimellitic acid (4-MET) and 10-methacryloyloxydecyl dihydrogen phosphate (MDP), with atelocollagen as a triple-helical peptide model. The STD NMR measurement was performed by adding 4-MET or MDP to the atelocollagen solution. Results: When the atelocollagen was saturated, the STD signals were detected in the MDP spectrum for the protons in the aliphatic chain when MDP was dissolved in DMSO. However, the STD signals disappeared when MDP was mixed with HEMA. No STD signal was visible for the 4-MET ligand samples in either DMSO or for the HEMA blend sample. Discussion: The interaction of MDP with atelocollagen is hydrophobic; however, the MDP-HEMA blend may form an aggregate in the atelocollagen solution, which would suppress the hydrophobicity of MDP. The formation of the MDP-HEMA aggregate may compromise the MDP-collagen interaction, and leave the collagen fibrils unprotected by MDP and HEMA. Unstable chemical interaction of the monomers with the exposed collagen may deteriorate hybrid layer integrity and strong dentin bonding.
PMID: 24440604 [PubMed - as supplied by publisher]
[NMR paper] Saturation transfer difference NMR for fragment screening.
Saturation transfer difference NMR for fragment screening.
Related Articles Saturation transfer difference NMR for fragment screening.
Curr Protoc Chem Biol. 2013 Dec 1;5(4):251-68
Authors: Begley DW, Moen SO, Pierce PG, Zartler ER
Abstract
Fragment screening by saturation transfer difference nuclear magnetic resonance (STD-NMR) is a robust method for identifying small molecule binders and is well suited to a broad set of biological targets. STD-NMR is exquisitely sensitive for detecting weakly binding compounds (a common characteristic of...
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01-07-2014 11:16 PM
[NMR paper] Specific RNA-protein interactions detected with saturation transfer difference NMR.
Specific RNA-protein interactions detected with saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.landesbioscience.com-icon-pubmed-Landesbioscience2.jpg Specific RNA-protein interactions detected with saturation transfer difference NMR.
RNA Biol. 2013 Jul 30;10(8)
Authors: Harris KA, Shekhtman A, Agris PF
Abstract
RNA, at the forefront of biochemical research due to its central role in biology, is recognized by proteins through various mechanisms. Analysis of the...
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08-21-2013 08:49 PM
[Question from NMRWiki Q&A forum] Saturation transfer difference TROSY
Saturation transfer difference TROSY
Has anyone added a pulse scheme for cross saturation to their TROSY for Bruker platform?
Could you share a pulse sequence if you have one?
Thanks!
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05-18-2013 09:22 AM
[NMR paper] Monomer-collagen interactions studied by saturation transfer difference NMR.
Monomer-collagen interactions studied by saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-sage.gif Related Articles Monomer-collagen interactions studied by saturation transfer difference NMR.
J Dent Res. 2013 Mar;92(3):284-8
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagami J
Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts....
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04-09-2013 06:31 PM
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
J Biol Inorg Chem. 2011 Apr 3;
Authors: Teixeira JM, Dias DM, Cañada FJ, Martins JA, André JP, Jiménez-Barbero J, Geraldes CF
The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD),...
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04-05-2011 10:22 PM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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12-01-2010 06:56 PM
[NMR paper] Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experim
Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Related Articles Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Proteins. 2004 Aug 1;56(2):346-53
Authors: Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M
Saturation transfer difference...
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11-24-2010 10:01 PM
Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed int
Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
Related Articles Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
Chem Commun (Camb). 2010 Sep 13;
Authors: Wagstaff JL, Vallath S, Marshall JF, Williamson RA, Howard MJ
We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in...