Ferulic acid, a natural phenolic compound, as a potential inhibitor for collagen fibril formation and its propagation.

Excess accumulation of collagen (fibrosis) is the hallmark of many fibrotic diseases such as keloids, hypertrophic scars, etc. The inhibition of collagen fibrillation during its accumulation is a therapeutic way to limit the fibrosis. Herein, the effect of Ferulic acid (FA), a natural phenolic acid compound, on collagen fibrillation is studied using biophysical methods. Optical density (OD) and microscopic analysis indicate that FA inhibits collagen self-association, and the inhibitory efficiency depends on the concentration and temperature. The absence of an increase in OD for matured collagen fibrillar solution upon addition of FA followed by collagen solution indicates that FA could also terminates the progression of preformed collagen fibrils. Spectroscopic measurements indicate that collagen retains its unique triple helical structure in the presence of FA. Saturation Transfer Difference NMR suggests that FAs are in proximity to collagen while fluorescence quenching upon addition of FA proposes that FA most likely binds to the telopeptide regions of collagen. Enzymatic studies suggest that FA protects collagen from enzymatic degradation. The current study demonstrates that FA is a potential inhibitor of collagen fibrillation and its propagation and thus it can be considered for therapeutic studies to make FA as a remedy for the plaques related to collagen deposition.