Effect of Peptide and Guest Charge on the Structural, Mechanical and Release Properties of β-Sheet Forming Peptides

• DOI: 10.1021/la303328p
• Publication Date: 2012-10-23T03:07:15Z
• Authors: D. Roberts; C. Rochas; A. Saiani; A. F. Miller
• Keywords: Beta sheet

The effect of peptide charge on the self-assembly, gelation behavior, and model drug release profiles has been explored here for three octa-peptides, VEVKVEVK (VEK2), VKVKVEVK (VEK3), VEVEVKVE (VEK1), that carry a net 0, +2, -2 at neutral pH, respectively. Transparent, self-supporting hydrogels were found to form above critical concentration when modulus was >1 this independent sign charge. TEM, SAXS, shear rheology revealed there no differences in hydrogel structure or mechanical properties peptides same carried modulus. All dense fibrillar networks formed by β-sheet rich single fibers where lateral aggregation occurred increased with decreasing Such behavior correlate an increase properties, demonstrating fiber is inextricably linked these hydrogels. Two hydrophilic molecules, namely napthol yellow (NY) martius (MY), subsequently incorporated within VEK1 VEK3 pH 7 although they did not self-assembly molecular level, level observed and, therefore, each molecule from monitored over time shown be controlled Fickian diffusion rate, D, dependent ratio between overall effective charges peptide, i.e., network, guest but ranges investigated. This work highlights possibility controlling rate small molecules manipulating as well charged state self-assembling peptide.