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Current Medicinal Chemistry
ISSN (Print): 0929-8673
ISSN (Online): 1875-533X
DOI: 10.2174/092986712802430018      Price:  $58

Physicochemical Strategies for Inhibition of Amyloid Fibril Formation: An Overview of Recent Advances

Author(s): 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.