Combinatorial peptide synthesis on different solid phases and their thermographic investigation on CO2-binding affinity

In order to reduce or even avoid carbon dioxide emissions into the environment, certain peptide sequences have been investigated regarding their binding affinity for CO 2 . Existing methods of solid-phase peptide synthesis were adopted and transferred to amino-functionalized glass slides. Here, a combinatorial method was used to produce peptide arrays from different amino acids. Carboxylases are known for the fixation of CO 2 from the atmosphere in plants during photosynthesis. These enzymes served as a model for the bio-inspired peptide sequences. The resulting collection of 300 different peptide sequences was examined for the binding affinity of CO 2 . The investigation was carried out in a sealed box flooded with CO 2 using a thermographic camera, which can detect the endo- or exothermic heat of reactions that is absorbed or released by the binding of CO 2 to the peptides. Two conspicuous tripeptides were found based on the model of carboxylases. By repeatedly synthesizing this sequence on different solid phases, the thermographic anomalies could be reproducibly observed.