Hydrophobicity regulates self-assembly behavior of binding-induced fibrillogenesis peptides

Tetrasulfide bond boosts the anti-tumor efficacy of dimeric prodrug nanoassemblies

“…The addition of sulfur atoms and methylene groups increased the molecular hydrophobicity, and as shown in Data S3 , the log p values of CTX and the four prodrugs were CTX (4.20) < γ-2S-2CTX (11.04) < γ-3S-2CTX (11.64) < γ-4S-2CTX (12.23) < δ-4S-2CTX (13.12). To investigate whether the high hydrophobicity of γ-4S-2CTX and δ-4S-2CTX played a role in their superior self-assembly, 22 we synthesized δ-4C-2CTX by replacing the tetrasulfide bond of δ-4S-2CTX with carbon atoms ( Data S2 ). δ-4C-2CTX has a similar log p value (13.78) to δ-4S-2CTX.…”

Metal-Chelating Self-Assembling Peptide Nanofiber Scaffolds for Modulation of Neuronal Cell Behavior

“…Other approaches propose the combination of peptide motifs with non-peptidic components such as polymers or hydrophobic segments to induce predicted self-assembly [4]. Particularly, peptide amphiphiles (PAs), in which hydrophobic groups are attached to hydrophilic peptide sequences, are capable of self-assembling into different nanostructures such as micelles, nanofibers, and nanotubes [4][5][6]. The self-assembly process is driven by non-covalent interactions including hydrogen bonding, hydrophobic and electrostatic interactions, and van der Waals forces [4,7].…”