Abstract
N-terminal acetylation is a commonly used modification technique for synthetic peptides, mostly applied for reasons of enhanced stability, and in many cases regarded as inconsequential. In engineered biosilification - the controlled deposition of silica for nanotechnology applications by designed peptides - charged groups often play a deciding role. Here we report that changing the charge by acetylation of a 14-amino acid leucine-lysine (LK) peptide dramatically changes the morphology of precipitated biosilica; acetylated LK peptides produce nano-spheres, whereas nano-wires are precipitated by the same peptide in a non-acetylated form. By using interface-specific vibrational spectroscopy and coarse-grained molecular simulations, we show that this change in morphology is not the result of modified peptide-silica interactions, but rather caused by the stabilization of the hydrophobic core of peptide aggregates created by the removal of a peptide charge upon acetylation. These results should raise awareness of the potential impact of N-terminal modifications in peptide applications.
| Original language | English |
|---|---|
| Journal | Journal of Peptide Science |
| Volume | 23 |
| Issue | 2 |
| Pages (from-to) | 141-147 |
| Number of pages | 7 |
| ISSN | 1075-2617 |
| DOIs | |
| Publication status | Published - 2017 |
Keywords
- Acetylation
- Molecular dynamics
- Peptides
- Sum frequency generation