Effect of ligands with different affinity on albumin fibril formation

Inhibition of amyloid formation of bovine hemoglobin by bioactive phenolic acids: an elaborate investigation into their binding properties with the protein using multi-spectroscopic and computational techniques

“…A study reported that potent fibril inhibition could be successful with stronger protein–ligand binding due to higher stabilization of the protein structure. 135 This higher binding affinity of CA towards BHb implied that CA could preserve the structural integrity of BHb, leading to reduced fibrillation. Another study based on anti-fibrillating properties of resveratrol, curcumin, quercetin, vitamin C, and N -acetyl-cysteine was performed against amyloid-forming model protein stefin B.…”

Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models

“…Change in the value of α always affects the thermodynamics of equilibrium fibril formation, decreasing the fibril yield as shown in Figure 7 ; nevertheless, this can leave unnoticed in experiments in the case of weak binding or low K F values. Hence, monomer-binding species act as thermodynamic inhibitors of fibrillation [ 68 ], but of course, they also affect the kinetic parameters of this process. Strong binders changing the fibril yield should be able to disrupt the preformed fibrils at least partially.…”