| 内容提要: |
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.
This review discusses and examines the physicochemical strategies employed in inhibiting protein aggregation and amyloid fibril formation in recent literature. However, a satisfactory inhibition effect on aggregation and fibrillation has not been achieved for many proteins. What’s more, the molecular information and interaction mechanism involved in protein aggregation and amyloid inhibition are not clear. Continuous development of creative approaches and chemistries as well as analytical technologies is urgently needed for an ultimate solution of protein aggregation in biopharmaceuticals and clinical pathology. |