Glycation of Lys-16 and Arg-5 in amyloid-β and the presence of Cu play a major role in the oxidative stress mechanism of Alzheimer's disease.

Extensive research has linked the amyloid-beta (Aβ) peptide to neurological dysfunction in Alzheimer's disease (AD). Insoluble Aβ plaques in the AD patient brain contain high concentrations of advanced glycation end-products (AGEs) as well as transition metal ions. This research elucidated the roles of Aβ, sugars, and Cu in the oxidative stress mechanism of AD at the molecular level.

Purine biosynthetic intermediate-containing ribose-phosphate polymers as evolutionary precursors to RNA.

The RNA world hypothesis proposes that RNA once functioned as the principal genetic material and biological catalyst. However, RNA is a complex molecule made up of phosphate, ribose, and nucleobase moieties, and its evolution is unclear. Yakhnin has proposed a period of prebiotic chemical evolution prior to the advent of replication and Darwinian evolution, in which macromolecules containing polyols joined by phosphodiester linkages underwent spontaneous transesterification reactions with selection for stability.

Ribose 5-phosphate glycation reduces cytochrome c respiratory activity and membrane affinity.

Spontaneous glycation of bovine heart cytochrome c (cyt c) by the sugar ribose 5-phosphate (R5P) weakens the ability of the heme protein to transfer electrons in the respiratory pathway and to bind to membranes. Trypsin fragmentation studies suggest the preferential sites of glycation include Lys72 and Lys87/88 of a cationic patch involved in the association of the protein with its respiratory chain partners and with cardiolipin-containing membranes. Reaction of bovine cyt c with R5P (50 mM) for 8 h modified the protein in a manner that weakened its ability to transfer electrons to cytochrome oxidase by 60%.

Ribose sugars generate internal glycation cross-links in horse heart myoglobin.

Glycation of horse heart metmyoglobin with d-ribose 5-phosphate (R5P), d-2-deoxyribose 5-phosphate (dR5P), and d-ribose with inorganic phosphate at 37°C generates an altered protein (Myo-X) with increased SDS-PAGE mobility. The novel protein product has been observed only for reactions with the protein myoglobin and it is not evident with other common sugars reacted over a 1 week period. Myo-X is first observed at 1-2 days at 37°C along with a second form that is consistent in mass with that of myoglobin attached to several sugars.

Maillard reaction of ribose 5-phosphate generates superoxide and glycation products for bovine heart cytochrome c reduction.

Ribose 5-phosphate (R5P) is a sugar known to undergo the Maillard reaction (glycation) at a rapid rate. In a reaction with the lysines of bovine heart cytochrome c, R5P generates superoxide (O2-) that subsequently reduces ferri-cytochrome c to ferro-cytochrome c. The rate equation for the observed cytochrome c reduction is first order in respect to cytochrome c and half order in respect to R5P.

Importance of platinum(II)-assisted platinum(IV) substitution for the oxidation of guanosine derivatives by platinum(IV) complexes.

Guanosine derivatives with a nucleophilic group at the 5' position (G-5') are oxidized by the Pt (IV) complex Pt( d, l)(1,2-(NH 2) 2C 6H 10)Cl 4 ([Pt (IV)(dach)Cl 4]). The overall redox reaction is autocatalytic, consisting of the Pt (II)-catalyzed Pt (IV) substitution and two-electron transfer between Pt (IV) and the bound G-5'. In this paper, we extend the study to improve understanding of the redox reaction, particularly the substitution step.

The multiple Maillard reactions of ribose and deoxyribose sugars and sugar phosphates.

Ribose 5-phosphate (R5P) undergoes the Maillard reaction with amines at significantly higher rates than most other sugars and sugar phosphates. The presence of an intramolecular phosphate group, which catalyzes the early stages of the Maillard reaction, provides the opportunity for the R5P molecule to undergo novel reaction paths creating unique Maillard products. The initial set of reactions leading to an Amadori product (phosphorylated) and to an alpha-dicarbonyl phosphate compound follows a typical Maillard reaction sequence, but an observed phosphate hydrolysis accompanying the reaction adds to the complexity of the products formed.

The catalytic effect of Mg2+ and imidazole on the decomposition of 5-phosphoribosyl-alpha-1-pyrophosphate in aqueous solution.

The rate of decomposition of aqueous solutions of 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP) is greatly enhanced by the presence of certain divalent ions. High levels of Mg(2+) were shown to increase the rate of phosphate removal from PRPP by factors greater than 100-fold. The combined action of Mg(2+) and a nitrogenous compound (imidazole was employed in this study) increases the degradation rate constants by up to 1000-fold.