Enantiospeci c biorecognition interactions are key to many biological events. Commonly, bio-a nity values, measured in these processes, are higher than those calculated by available methods. We report here the rst direct measurement of the interaction force between right and left handed helical polyalanine peptides using atomic force microscope (AFM) and calculations based on a simple theoretical model. A force difference of 60pN between same and opposite enantiomer interactions is measured. Additional measurements show spin dependency and fast decay of the interaction term, consistent with spin exchange interactions. This short range enantiospeci c interaction term is especially relevant in crowded biological systems. The results shed light on the importance of spin and exchange interactions in biological processes, providing explanation to the discrepancies between past calculations and experiments.
Main TextNature is based on chiral molecules, namely molecules that appear in two forms, enantiomers, that are mirror images of each other. Interestingly, chiral biomolecules, like proteins and sugars appear in Nature mainly as one enantiomer. The origin of "homo chirality" in Nature, was -and is -discussed very intensively in the literature 1 . However, the focus of this work is related to a more fundamental question, i.e., why did Nature preserve chirality so persistently over the many millions years of evolution? In other words, does chirality per se, independent on the speci c handedness, provide properties that serve an important role in Life?The ability of biological molecules to interact selectively with each other is at the heart of all biological processes and the basis of many pharmaceutical concepts. Two important properties -related to chirality -characterize interactions in nature, i.e., very strong enantioselectivity