Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II.

Previous work has examined the effects of such factors as pH and peptide concentration on the self-assembly of ionic-complementary peptides. This work focused on the effect of sodium chloride on the molecular self-assembly of an ionic-complementary peptide EAK16-II (AEAEAKAKAEAEAKAK). Surface tensions and dimensions of the self-assembled nanostructures were determined for a wide range of peptide and sodium chloride concentrations using axisymmetric drop shape analysis-profile (ADSA-P) and atomic force microscopy (AFM), respectively.

Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV.

Atomic force microscopy (AFM) and axisymmetric drop shape analysis-profile (ASDA-P) were used to investigate the mechanism of self-assembly of peptides. The peptides chosen consisted of 16 alternating hydrophobic and hydrophilic amino acids, where the hydrophilic residues possess alternating negative and positive charges. Two types of peptides, AEAEAKAKAEAEAKAK (EAK16-II) and AEAEAEAEAKAKAKAK (EAK16-IV), were investigated in terms of nanostructure formation through self-assembly.