Physicochemical Strategies for Inhibition of Amyloid Fibril Formation: An Overview of Recent Advances
R. Liu, R. Su, M. Liang, R. Huang, M. Wang, W. Qi and Z. He
Pages 4157-4174 (18)
Protein aggregation and amyloid fibrillation can lead to several serious human diseases and protein drug ineffectiveness. The
complexity and dynamics of protein folding present unique challenges for elucidating the molecular mechanisms involved in protein
aggregation and designing effective amyloid inhibitors. Continuous development of creative approaches to identify an ultimate solution
for controlling protein aggregation in biopharmaceuticals and clinical pathology is clearly required. This review describes and discusses
the most recent advances on the physicochemical strategies for inhibiting protein aggregation and amyloid fibrillation, with emphasis on
giving a brief overview of creative approaches and chemistries used. Physical strategies for inhibiting amyloid fibril formation, including
high hydrostatic pressure, low temperature, and laser irradiation, are critically evaluated. Recent advances in chemical strategies
including small molecules, metal chelators, and nanomaterials, as well as in the use of biomolecules (peptide, protein, nucleic acid, and
saccharide) as amyloid inhibitors, are also highlighted.
Amyloid inhibition, amyloid-related disease, protein aggregation, assembly, fibril, hydrostatic pressure, laser irradiation, metal
chelator, nanomaterial, biomolecule, peptide, protein, nucleic acid, saccharide, polyphenols.
State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, P. R. China.