Abstract
Peptides of alternating charge and hydrophobic amino acids have a tendency to adopt unusually stable β‐sheet structures that can form insoluble macroscopic aggregates under physiological conditions. In this study, analogues of a well‐known self‐assembling peptide, characterized by the same polar/nonpolar periodicity but with different residues, were designed to study the relationship between sequence, conformation in solution and film‐forming capacity in saline solution. Peptide conformation, evaluated by circular dichroism, correlated with film forming capacity observed by inverted optical microscopy after addition of saline solution and subsequent drying. We found that polar/nonpolar periodicity of several analogues is not criterion enough to induce β‐sheet and thus film formation and that conformations different from β‐sheet also allow self‐assemblage. Furthermore, addition of the short adhesive sequence RGD to a known self‐assembling sequence was shown to not prevent the self‐assembling process. This finding might prove useful for the design of biomimetic scaffolds. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 906–915, 2008.
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