Abstract
Glycation of various biomolecules contributes to structural changes and formation of several high molecular weight fluorescent and non-fluorescent, advanced glycation end products (AGEs). AGEs and glycation are involved in various health complications. Synthetic medicines, including metformin, have several adverse effects. Natural products and their derivatives are used in the treatment of various diseases due to their significant therapeutic qualities. Allium sativum (garlic) is used in traditional medicines because of its antioxidant, anti-inflammatory, and anti-diabetic properties. This study aimed to determine the anti-glycating and AGEs inhibitory activities of garlic. Biochemical and biophysical analyses were performed for in vitro incubated human serum albumin (HSA) with 0.05 M of glucose for 1, 5, and 10 weeks. Anti-glycating and AGEs inhibitory effect of garlic was investigated in glycated samples. Increased biochemical and biophysical changes were observed in glycated HSA incubated for 10 weeks (G-HSA-10W) as compared to native HSA (N-HSA) as well as glycated HSA incubated for 1 (G-HSA-1W) and 5 weeks (G-HSA-5W). Garlic extract with a concentration of ≥6.25 µg/mL exhibited significant inhibition in biophysical and biochemical changes of G-HSA-10W. Our findings demonstrated that garlic extract has the ability to inhibit biochemical and biophysical changes in HSA that occurred due to glycation. Thus, garlic extract can be used against glycation and AGE-related health complications linked with chronic diseases in diabetic patients due to its broad therapeutic potential.
Highlights
IntroductionNon-enzymatic glycation reaction involves the binding of sugars (glucose, fructose, ribose, etc.) to free ε-amino groups of proteins in the absence of enzymes
Non-enzymatic glycation reaction involves the binding of sugars to free ε-amino groups of proteins in the absence of enzymes
An alkaline reagent test was used to validate the presence of flavonoids in several plant extracts
Summary
Non-enzymatic glycation reaction involves the binding of sugars (glucose, fructose, ribose, etc.) to free ε-amino groups of proteins in the absence of enzymes. The reaction is classically covalent, in which a sugar protein complex is formed through N-glycoside bonding, via a cascade of chemical responses described by the chemist Maillard [1]. AGEs are endogenous compound groups formed by non-enzymatic reactions [2,3]. Glycation exerts structural alteration of proteins, adversely affecting their physiological functions. Normal physiologic conditions lead to progressive increase in AGE formation with aging [4]. The process is accelerated under hyperglycemic conditions and in other inflammatory diseases [5,6,7,8]. AGEs can even be ingested through food [9]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
