What question did this study set out to answer?

The research aims to identify and characterize peptide sequences from Temporin L that can self-assemble and mimic collagen.

March 13, 2026Open Access

Aromatic Residue-Rich Amino-terminal Segments of Temporin L Self-Assemble into Collagen-Mimetic Peptides with Cell-Adhesion Properties

Key Points

The research aims to identify and characterize peptide sequences from Temporin L that can self-assemble and mimic collagen.
Synthesized five peptides ranging from 4 to 8 residues derived from the amino-terminus of Temporin L.
Analyzed structural features using techniques like circular dichroism (CD) spectroscopy and ultrastructural studies.
Evaluated the adhesive properties of these peptides with HepG2 cells and assessed impacts of integrin inhibition.
T-6mer, T-7mer, and T-8mer displayed collagen-like triple-helical characteristics.
The T-8mer formed a hydrogel and demonstrated a rapid self-assembly with significant water saturation.
HepG2 cells adhered significantly to the T-6mer, T-7mer, and T-8mer, with adhesion compromised by integrin receptor antibodies.

Abstract

Intriguingly, 13-mer frog-peptide, temporin L (TempL) contains 50% aromatic residues within its first eight residues.Considering the role of aromatic residues in self-assembly of peptides and the potential of such peptides in biomedical applications, we envisaged to identify new short self-assembling peptides from the amino-terminus of TempL and characterize their structural and biological properties.Thus, starting from the 8 th to the 1 st residue of TempL, we synthesized, five 4-8 residue peptides (T-4mer to T-8mer).Different ultrastructural studies suggested nano-J o u r n a l P r e -p r o o f spherical/nano-fibrillar structures of these peptides.Remarkably, T-6mer, T-7mer and T-8mer exhibited polyproline type-II CD spectra of collagen-like triple-helical structure and sigmoidal melting curves like that we observed with rat-tail type-I collagen.Amazingly, the T-8mer peptide at 1.5% (w/v) forms hydrogel within an hour indicating its ability to form supramolecular assembly, saturated with water.We further studied collagen-mimetic nature of these TempL-derived peptides.HepG2 cells showed significant adhesions onto the coatings of T-6mer, T-7mer, T-8mer peptides and rat-tail type-I collagen which got compromised when these cells were pre-treated with antibody of collagen receptor, integrin 21.Interestingly, following the adhesions onto the surface of these TempL-derived peptides, cytoskeletal organization was induced in HepG2 cells like that observed in the presence of a collagen protein.Overall, the current results demonstrated the dissection of a frog-peptide, TempL with revelation of collagenmimetic peptides from its aromatic-residue rich amino-terminus.

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