Anti-glycation Effect of Gold Nanoparticles on Collagen
Gold nanoparticles (GNPs) have been reported to exhibit a variety of biological effects including antiinflammatory and anti-oxidant activities. The extent of an in vitro glycation reaction mixture of collagen and glycolaldehyde was assayed to investigate the inhibition of glycolaldehye-derived advanced glycation end products (glycol-AGEs) formation with GNPs in collagen, which is a major protein component of the human dermis. GNP-treated collagen showed significantly less glycation (56.3±4.2%) than an untreated glycation control. Moreover, GNP-treated glycation in a collagen lattice model significantly decreased the AGEs distribution in the model system. Taken together, these results suggest that GNPs have the potential for use in the prevention of glycation-induced skin aging.
GOLD NANOPARTICLES
Ji-hoon Kim, Chung-Oui Hong, Yun-chang Koo, Hee-Don Choi, and Kwang-Won Lee
10/2/20242 分钟阅读
Source: Anti-glycation Effect of Gold Nanoparticles on Collagen
Skin aging is the result of genetic intrinsic chronological aging and extrinsic aging due to external factors. One of the causes of aging is the appearance of advanced glycation end products (AGEs). AGEs are formed by chemical reaction of carbohydrates with protein in a process known as the Maillard or glycation reaction. This reaction begins with adduction of a reducing sugar to an amino group in protein, typically the ε-amino group of a lysine residue, to form a Schiff base, which then rearranges to an Amadori compound. The Amadori product is a precursor to AGEs, which are a more permanent, irreversible modification of proteins. AGEs modifications of proteins may lead to alterations in normal function by inducing cross-linking of extracellular matrices. In the current study, glycolaldehye-derived AGEs (GA-AGEs) was used as a source of AGEs. It appears that short chain sugars such as GA could play an important role as intermediates in the formation of AGE structures in the glycation reaction. Based on immunoreactivity, GA-pyridine having a GA-AGE structure is reported to be the most significant AGE for cartilage degredation though AGE-its specific receptor (RAGE)- oxidative stress axis.
A number of compounds have been introduced as AGE inhibitors based on their inhibition of AGE formation during incubation of proteins with glucose in vitro. These inhibitors vary widely in structure, the common theme being their nucleophilicity or reactivity with reactive carbonyl intermediates in AGE formation. Aminoguanidine (AG) has been suggested as a representative agent for the inhibition of glycation, although clinical trials for this compound were stopped due to reported side effects. Gold nanoparticles (GNPs) have been reported to exhibit a variety of biological activities, including anti-imflammatory and anti-oxidant activities. GNPs, which represent an emerging nanomedicine, are renowned for their promising therapeutic possibilities, which include biocompatibility, high surface reactivity, anti-oxidation and plasmon resonance.
In the present study, we investigated the inhibitory effect on AGE formation with GNPs in glycation between collagen, a major protein component of the human dermis and GA.
