The status of glycation in protein aggregation.

Int J Biol Macromol

Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; UNESCO Chair on Interdisciplinary Research in Diabetes at University of Tehran, Iran; Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran. Electronic address:

Published: July 2017

Protein crucial function and flexibility directly depend on its whole structure which is determined by the native distribution of structural elements. Any disturbances in a protein architecture leads to many kind of abnormalities and intra- or extracellular accumulation of misfolded proteins which are the basis of conformational diseases. Glycation is one of the most important unwanted post-translational modifications (PTM) which modifies protein three dimensional decoration and triggers its abnormalities. In current review, we take a look at the brief history of protein glycation, its mechanism and kinetics, glycation consequences and toxic products and its involvement in protein chemical modification, aggregation amyloids and fibril formation and different mechanisms induced by such alterations.

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http://dx.doi.org/10.1016/j.ijbiomac.2015.12.085DOI Listing

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