[NMR paper] A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Related ArticlesA new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Abstract
NMR is ideal for characterizing non-enzymatic protein glycation, including AGEs (advanced glycation end products) underlying tissue pathologies in diabetes and ageing. Ribose, ribose-5-phosphate (R5P) and ADP-ribose (ADPR) could be significant and underinvestigated biological glycating agents especially in chronic inflammation. Using [U-13C]ribose we have identified a novel glycoxidation adduct, 5-deoxy-5-desmethylpronyl-lysine, "norpronyl-lysine", as well as numerous free ketones, acids, and amino group reaction products. Glycation by R5P and ADPR proceeds rapidly, with R5P generating a brown precipitate with PLL within hours. Solid state NMR (ssNMR) 13C-13C correlation spectroscopy identifies several crosslinking adducts such as the newly identified norpronyl-lysine, in situ, from the glycating reaction of 13C5-ribose with collagen. The same adducts are also identifiable after reaction of collagen with R5P. We also demonstrate for the first time bio-amine (spermidine, N-acetyl lysine, poly-L-lysine (PLL)) catalyzed ribose 2-epimerization to arabinose at physiological pH. This work raises the prospect of advancing understanding of the mechanisms and consequences of glycation in actual tissues, in vitro or even ex vivo, using NMR isotope-labelled glycating agents, without analyses requiring chemical or enzymatic degradations, or prior assumptions about glycation products.
PMID: 24517485 [PubMed - as supplied by publisher]
[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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Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi102012j/aop/images/medium/bi-2010-02012j_0006.gif
Biochemistry
DOI: 10.1021/bi102012j
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Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Biochemistry. 2011 Feb 16;
Authors: Mealman TD, Bagai I, Singh P, Goodlet DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM
The E. coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the...
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02-18-2011 08:07 PM
[NMR paper] Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic stu
Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Related Articles Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Magn Reson Chem. 2004 Apr;42(4):369-72
Authors: Iuga A, Brunner E
Solid-state 31P NMR spectroscopy was applied to measure the isotropic chemical shifts, chemical shift anisotropies and asymmetry parameters of three phosphorylated amino acids, O-phospho-L-serine, O-phospho-L-threonine and O-phospho-L-tyrosine. The...
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[NMR paper] 1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible in
1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible inhibitors of InhA reductase of Mycobacterium tuberculosis.
Related Articles 1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible inhibitors of InhA reductase of Mycobacterium tuberculosis.
Chemistry. 2003 May 9;9(9):2034-8
Authors: Broussy S, Coppel Y, Nguyen M, Bernadou J, Meunier B
Isoniazid (INH) is easily oxidized with manganese(III) pyrophosphate, a chemical model of the KatG protein involved in activation of INH inside the...
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Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...
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[NMR paper] In vivo detection and characterization of protein adducts resulting from bioactivatio
In vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by 19F NMR: chlorotrifluoroethene and tetrafluoroethene.
Related Articles In vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by 19F NMR: chlorotrifluoroethene and tetrafluoroethene.
Chem Res Toxicol. 1992 Jan-Feb;5(1):34-41
Authors: Harris JW, Dekant W, Anders MW
Several haloalkenes are selective nephrotoxins. The bioactivation of nephrotoxic...
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[NMR paper] Structural characterization of the interactions of optimized product inhibitors with
Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
J Mol Biol. 1999 Jun 4;289(2):385-96
Authors: Cicero...
A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
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