Lawrence Berkeley National Laboratory
Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers.
- Author(s): Eckshtain-Levi, Meital
- Capua, Eyal
- Refaely-Abramson, Sivan
- Sarkar, Soumyajit
- Gavrilov, Yulian
- Mathew, Shinto P
- Paltiel, Yossi
- Levy, Yaakov
- Kronik, Leeor
- Naaman, Ron
- et al.
Published Web Locationhttps://doi.org/10.1038/ncomms10744
Chirality-induced spin selectivity is a recently-discovered effect, which results in spin selectivity for electrons transmitted through chiral peptide monolayers. Here, we use this spin selectivity to probe the organization of self-assembled α-helix peptide monolayers and examine the relation between structural and spin transfer phenomena. We show that the α-helix structure of oligopeptides based on alanine and aminoisobutyric acid is transformed to a more linear one upon cooling. This process is similar to the known cold denaturation in peptides, but here the self-assembled monolayer plays the role of the solvent. The structural change results in a flip in the direction of the electrical dipole moment of the adsorbed molecules. The dipole flip is accompanied by a concomitant change in the spin that is preferred in electron transfer through the molecules, observed via a new solid-state hybrid organic-inorganic device that is based on the Hall effect, but operates with no external magnetic field or magnetic material.