Investigation on structure and properties of a novel designed peptide

Abstract

Although the existing design principle of full-sequence ionic complement is convenient for the development of peptides, it greatly constrains the exploration of peptides with other possible assembly mechanisms and different yet essential functions. Herein, a novel designed half-sequence ionic complementary peptide (referred to as P9), AC-Pro-Ser-Phe-Asn-Phe-Lys-Phe-Glu-Pro-NH 2 , is reported. When transferred from pure water to sodium chloride solution, P9 underwent a dramatic morphological transformation from globular aggregations to nanofibers. Moreover, the rheological experiment showed that the P9 could form a hydrogel with a storage modulus of about 30 Pa even at very low peptide concentration (0.5% (wt/vol)). The P9 hydrogel formed in salt solution could recover in a period of about 1,800 sec, which is faster than that in the pure water. The data suggested that the half-sequence, ionic complementary peptide might be worthy of further research for its special properties.

Accessing Highly Tunable Nanostructured Hydrogels in a Short Ionic Complementary Peptide Sequence via pH Trigger

“…Variation was observed in the extent of ellipticity around 235 nm with the change in the pH value. At pH 2.0 and 12.0, the CD spectra indicate a high intensity of ellipticity due to the π–π* transition of the naphthoxyl group in the aromatic peptide, but with the change in pH to other values in the 5.0–10.0 range, the spectra showed β-sheet structures but the extent of ellipticity reduces, which is probably due to the twisting or unordered structures present in the hydrogels . These results corroborate well with the recent report by our group, where the coassembly of the oppositely charged collagen-inspired peptide sequences resulted in formation of a cross-β-sheet structure due to the electrostatic interaction .…”

“…At pH 2.0 and 12.0, the CD spectra indicate a high intensity of ellipticity due to the π−π* transition of the naphthoxyl group in the aromatic peptide, but with the change in pH to other values in the 5.0−10.0 range, the spectra showed β-sheet structures but the extent of ellipticity reduces, which is probably due to the twisting or unordered structures present in the hydrogels. 69 These results corroborate well with the recent report by our group, where the coassembly of the oppositely charged collagen-inspired peptide sequences resulted in formation of a cross-β-sheet structure due to the electrostatic interaction. 64 This variation suggests that although the peptide is forming the β-sheet-like structures in general, the selfassembled structures were twisted and disordered, resulting in heterogeneous structures in the hydrogels.…”

Design of Self-Assembling Peptides and Their Biomedical Applications

“…In another study, Zhao and coworkers have found that when peptide P9 was transferred from pure water to sodium chloride solution [15], it underwent a dramatic morphological transformation from globular aggregations to nanofibers. Moreover, the theological experiment showed that the P9 could form a hydrogel even at a low peptide concentration (0.5% [wt/vol]).…”

Supramolecular Hydrogels for Regenerative Medicine

“…This amphiphilic PSFCFLFEP peptide also includes a proline to increase the formation of fibrils and to induce the β-turn. Hydrogels prepared with this peptide showed shear moduli of around 20 Pa, and addition of sodium chloride increased the moduli approximately tenfold [91]. The fibrils were able to gradually release hydrophobic model compounds such as pyrenes.…”