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Updated: Mar 27, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Modulating self-assembly behavior of a salt-free peptide amphiphile (PA) and zwitterionic surfactant mixed system
Han Zhang1, Jichao Sun1, Xia Xin2
1Key Laboratory of Colloid and Interface Chemistry (Shandong University), Ministry of Education, Shanda nanlu No. 27, Jinan 250100, PR China.
Abstract:
A salt-free surfactant system formed by a peptide amphiphile with short headgroup (PA,C16-GK-3) and a zwitterionic surfactant (dodecyldimethylamine oxide, C12DMAO) in water has been systematically investigated. The microstructures and properties of C16-GK-3/C12DMAO mixed system were characterized using a combination of microscopic, scattering and spectroscopic techniques, including transmission electron microscopy (TEM), field emission-scanning electron microscopy (FE-SEM), atomic force microscopy (AFM), Fourier transform infrared (FT-IR), circular dichroism (CD) and rheological measurements. Rich phase transitions have been observed by adjusting the concentration of C16-GK-3. Investigation of the hydrogels of C16-GK-3/C12DMAO with TEM, SEM and AFM showed that all of these hydrogels form nanobelts. The nanobelt formation is performed in a hierarchical manner: β-sheet peptides and C12DMAO first interact each other to form small aggregates, which then arrange themselves to form one dimensional (1D) left-handed ribbons. The ribbons further aggregated into flat and rigid nanobelts. We proposed a mechanism to interpret the self-assembly process according to the specific peptide structure as well as multiple equilibria between the hydrogen bonding interactions between the headgroups of C16-GK-3, between C12DMAO molecules and the headgroups of C16-GK-3, chirality of the amino acid residues and hydrophobic interactions of the alkyl chains.
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