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It has been found that the self‐assembling peptide RADA 16‐I forms a β‐sheet structure and self‐assembles into nanofibers and scaffolds in favor of cell growth, hemostasis and tissue‐injury repair. But its biophysical and morphological properties, especially for its β‐sheet and self‐assembling properties in heat‐ and pH‐denatured conditions, remain largely unclear. In order to better understand and design nanobiomaterials, we studied the self‐assembly behaviors of RADA16‐I using CD and atomic force microscopy (AFM) measurements in various pH and heat‐denatured conditions. Here, we report that the peptide, when exposed to pH 1.0 and 4.0, was still able to assume a typical β‐sheet structure and self‐assemble into long nanofiber, although its β‐sheet content was dramatically decreased by 10% in a pH 1.0 solution. However, the peptide, when exposed to pH 13.0, drastically lost its β‐sheet structure and …