Disruption of human serum albumin fibrils by a static electric field

Hydrophobic tail length plays a pivotal role in amyloid beta (25-35) fibril-surfactant interactions

“…Electromagnetic radiation also produces various effects on proteins, peptides, fibrils. Our laboratory has recently established that a static electric field causes maximum disruption of human serum albumin (HSA) fibrils at∼8 × 10 6 Vm – . Surfactants have also been found to modulate fibrillation of different proteins, peptides and to cause changes in their conformational preferences .…”

“…9 Amyloid fibrils have been found to be present in many forms and constituted of different fragments. The shortest but most toxic fragment so far reported is the amyloid beta (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) fragment (Ab [25][26][27][28][29][30][31][32][33][34][35] ) that undergoes accumulation to form amyloid plaques in the extracellular fluid of neuronal cells. [10][11][12] The amino acid sequence and structure of the peptide is provided in Figure 1 (PDB ID: 1QXC).…”

“…19 The 11 residue monomeric peptide mainly possessing random coil structure has been widely studied. Polyphenols are reported to stabilize the monomeric form of the Ab [25][26][27][28][29][30][31][32][33][34][35] peptide and inhibit fibrillation. 20,21 Interactions of the amyloid b (25-35) peptide with membranes have been found to be affected in the presence of flavonoids like rutin and quercetin.…”

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The amyloid b-peptide fragment comprising residues [25][26][27][28][29][30][31][32][33][34][35] ) is known to be the most toxic fragment of the full length Ab peptide which undergoes fibrillation very rapidly. In the present work, we have investigated the effects of the micellar environment (cationic, anionic, and nonionic) on preformed Ab 25-35 fibrils.

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Effect of fibrillation on the excited state dynamics of tryptophan in serum protein – A time-resolved fluorescence study

“…Recently, fibrillation of Human Serum Albumin (HSA), an important blood plasma protein has been investigated by several research groups [33][34][35][36][37]. Single tryptophan moiety (W214) in Human Serum Albumin (HSA) has been used as an internal fluorescent probe to report the local dynamics around it [38][39][40][41].…”