Deciphering Aspartyl Peptide Sweeteners Using the Ultimate Molecular Theory of Sweet Taste

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers
could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers. 1,2 Under the guidance of the sweet
receptor helix recognition theory 1, aspartyl/aminomalonyl peptide sweeteners are deciphered. Here it demonstrates that, this series of sweeteners has a
hydrogen-bond type hydrogen donor - hydrogen acceptor DH-B moiety and their DH-B is very special. Their B of the DH-B moiety is an oxygen of the carboxylic
group, which is widely accepted one. The DH of the DH-B moiety however is the NH of the aspartyl/aminomalonyl peptide, which is a selection for the first time to
the best of my knowledge. Even more unusual, their dynamic action acts through
the hydrogen on alpha carbon of aspartyl/aminomalonyl group. The receptor main and side grooves have different space characteristics in accepting sweet
molecules’ groups, which is elaborated in this paper. This unprecedented elucidation well explains the aspartyl/aminomalonyl peptide sweeteners’
phenomenon and, in return, strongly supports this sweet receptor helix recognition theory.