Does glycation really distort the peptide α-helicity?

Glycation End Products, Advanced / chemistry Glycosylation Magnetic Resonance Spectroscopy Mass Spectrometry Molecular Dynamics Simulation Peptides / chemical synthesis Protein Conformation, alpha-Helical Schiff Bases / chemistry Spectrum Analysis
Glycation Peptide α-Helix

Journal

International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578

Informations de publication

Date de publication:
15 May 2019
Historique:
received: 12 11 2018
revised: 23 12 2018
accepted: 31 01 2019
pubmed: 11 2 2019
medline: 25 7 2019
entrez: 11 2 2019
Statut: ppublish

Résumé

The understanding of the effect of non-enzymatic post-translational modifications on the protein structure is essential to unveil the molecular mechanisms underlying their related pathological processes. Among those modifications, protein glycation emerges as one of the main responsible for the development of diabetes-related diseases. While some reports suggest that glycation has a chaotropic effect, others indicate that it does not modify the protein structure. Here we aim to better clarify this effect and therefore, we have studied the effect of glycation mediated by ribose and methylglyoxal on a fifteen-residue model peptide, which readily undergoes a pH-induced coil-helix transition. Neither ribose nor methylglyoxal were able to induce the structuration of the peptide at physiological pH. Moreover, neither ribose nor methylglyoxal severely modified the α-helical structure acquired by the peptide at pH ~ 3. Among the different glycation products experimentally detected (i.e. the ribose-derived Schiff base; the Amadori compound; N

Identifiants

DOI: 10.1016/j.ijbiomac.2019.01.213 PMID: 30738904
pubmed: 30738904
pii: S0141-8130(18)36060-4
doi: 10.1016/j.ijbiomac.2019.01.213
pii:
doi:

Substances chimiques

Glycation End Products, Advanced 0
Peptides 0
Schiff Bases 0

Types de publication

Journal Article

Langues

eng

Pagination

254-266

Informations de copyright

Copyright © 2019 Elsevier B.V. All rights reserved.

Auteurs

Laura Mariño (L)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Rodrigo Casasnovas (R)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Rafael Ramis (R)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Bartolomé Vilanova (B)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Joaquín Ortega-Castro (J)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Juan Frau (J)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain.

Miquel Adrover (M)

Institut Universitari d'Investigació en Ciències de la Salut (IUNICS), Institut de Recerca en Ciències de la Salut (IdISBa), Departament de Química, Universitat de les Illes Balears, Ctra. Valldemossa km 7.5, E-07122 Palma de Mallorca, Spain. Electronic address: miquel.adrover@uib.es.

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Classifications MeSH

questionsmedicales.fr › Facteurs biologiques › Toxines biologiques › Produits terminaux de glycation avancée › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Métabolisme › Métabolisme glucidique › Glycosylation › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Analyse spectrale › Spectroscopie par résonance magnétique › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Spectrométrie de masse › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Sciences de l'information › Méthodologies informatiques › Simulation numérique › Simulation de dynamique moléculaire › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Acides aminés, peptides et protéines › Peptides › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure secondaire des protéines › Structure en hélice alpha › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Composés chimiques organiques › Imines › Bases de Schiff › Does glycation really distort the peptide α-helicity?
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Analyse spectrale › Does glycation really distort the peptide α-helicity?