Cold denaturation induces inversion of dipole and spin transfer in chiral peptide monolayers.

ABSTRACT: 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 ?-helix peptide monolayers and examine the relation between structural and spin transfer phenomena. We show that the ?-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.

SUBMITTER: Eckshtain-Levi M 

PROVIDER: S-EPMC4773432 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature