**4. Conclusions**

Enzymes such as amylase break down polysaccharides into monomeric sugars and thereby increase glucose concentrations in the serum. Furthermore, prolonged exposure of proteins to sugars and dicarbonyl intermediates led to the formation of advanced glycation end-products (AGEs). In our study, neutraceuticals molecules such as caffeic and coumaric acid bind with α-amylase and also inhibit the AGEs formation to a different extent. Caffeic acid possesses more inhibitory activity, which could be due to its planarity and hydrogen bonding potential. Van der Waals and hydrogen bonding are the major forces between the polyphenols–protein interactions. Molecular docking along with fluorescence quenching and synchronous fluorescence displayed the ability of phenolics to form stable complex with amylase. Moreover, these phenolics decrease AGE formation by inhibiting fructosamine. Furthermore, oxidation of proteins boosted the effect of glycation; caffeic and coumaric acid attenuate it by protecting thiol and carbonyl groups. The scheme for our probable mechanism for AGE inhibition is depicted in Figure 7. More research on similar structures along with in vivo studies is warranted to design inhibitors for diabetic complications.

**Figure 7.** Mechasnidtic pathway of caffeic and coumaric acid to inhibit advanced glycation endproducts (AGEs).

**Author Contributions:** Conceptualization, M.S.K.; validation M.S.K., M.S.A., A.M.H.A., N.A., N.O.A., A.M.A. and M.A.Z.; formal analysis, M.S.K., M.S.A., A.M.H.A., N.A., N.O.A., A.M.A. and M.A.Z.; funding acquisition writing—original draft preparation, M.S.K., M.S.A., A.M.H.A., N.A., N.O.A., A.M.A. and M.A.Z.; project administration, M.S.A.; funding acquisition, M.S.K. All authors have read and agreed to the published version of the manuscript.

**Funding:** MSK acknowledge the generous support from Research Supporting Project (RSP-2021/352) by King Saud University, Riyadh, Kingdom of Saudi Arabia.

**Institutional Review Board Statement:** Not Applicable.

**Informed Consent Statement:** Not Applicable.

**Data Availability Statement:** Data will be available on request to corresponding author.

**Acknowledgments:** MSK acknowledge the generous support from Research Supporting Project (RSP-2021/352) by King Saud University, Riyadh, Kingdom of Saudi Arabia.

**Conflicts of Interest:** The authors declare no conflict of interest.
