STM Studies of Synthetic Peptide Monolayers

TL;DR

This study employs scanning probe microscopy to analyze the structure of peptide monolayers, revealing their dense organization, submolecular features, and the effects of redox cofactors on imaging.

Contribution

First detailed STM imaging of synthetic peptide monolayers showing alpha helices and layer structure, with analysis of cofactors' impact on imaging.

Findings

Peptides form dense, uniform monolayers

Submolecular resolution reveals alpha helices

Redox cofactors do not significantly alter imaging quality

Abstract

We have used scanning probe microscopy to investigate self-assembled monolayers of chemically synthesized peptides. We find that the peptides form a dense uniform monolayer, above which is found a sparse additional layer. Using scanning tunneling microscopy, submolecular resolution can be obtained, revealing the alpha helices which constitute the peptide. The nature of the images is not significantly affected by the incorporation of redox cofactors (hemes) in the peptides.