Amyloid ‐like aggregation of designer bolaamphiphilic peptides: Effect of hydrophobic section and hydrophilic heads

In this study, we showed that a series of designer bolaamphiphilic peptides could undergo amyloid‐like aggregation even though they didn't possess typical β‐sheet secondary structure. Through systematic amino acid substitution, we found that for the self‐assembling ability, the number and species of amino acid in hydrophobic section could be variable as long as enough hydrophobic interaction is provided, while different polar amino acids as the hydrophilic heads could change the self‐assembling nanostructures with their aggregating behaviors affected by pH value change. Based on these results, novel self‐assembling models and aggregating mechanisms were proposed, which might provide new insight into the molecular basis of amyloid‐like aggregation. Designer bolaamphiphilic short peptides could self‐assemble into nanofibers or nanospheres with amyloid‐like properties. Hydrophobic section determined the ability of self‐assembly, but the length and amino acid components could be variable, while hydrophilic heads played an important role in affecting the self‐assembling structures and their aggregation behaviors.
Source: Journal of Peptide Science - Category: Biochemistry Authors: Tags: RESEARCH ARTICLE Source Type: research