Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537003 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 47 Pages |
Abstract
⺠A model mechanism for Cyt c native-like aggregation upon glycation is proposed. ⺠Methylglyoxal glycation reduces Cyt c conformational stability. ⺠The molecular mechanism relies on protein native-like aggregate stabilization. ⺠Monolayer experiments show a thermodynamically and kinetically favored process.
Keywords
1,2-Dimyristoyl-sn-glycero-3-phospho-l-serinedMPCMGHTOFDMPSGdnHClACNMAGEAICSECCID1,2-dimyristoyl-sn-glycero-3-phosphocholineAcetonitrileConformational diseasecollision induced dissociationLipid monolayertime of flightAgecytochrome cMALDIMethylglyoxalAdvanced glycation end-productAkaike Information CriteriaGuanidinium hydrochlorideHydroimidazoloneSize exclusion chromatographyGlycation
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Luis M.A. Oliveira, Ricardo A. Gomes, Dennis Yang, Sarah R. Dennison, Carlos FamÃlia, Ana Lages, Ana V. Coelho, Regina M. Murphy, David A. Phoenix, Alexandre Quintas,