Amino Acid Derivatives of Tetrathiafulvalene and Their N–H···O Peptide Bond Dipoles‐Templated Solid State Assemblies

We report on a series of amino acid derivatives of tetrathiafulvalene as well as on the structure‐directing abilities of their peptide residues in the crystalline solid state to stabilize patterns of interactions such as β strands and sheet motifs. Characteristic hydrogen‐bonding motifs are indeed identified within ethylenedithiotetrathiafulvalene (EDT‐TTF) and dimethyltetrathiafulvalene (Me 2 ‐TTF) based compounds 1 – 5 . Esters 1 – 3 contain hydrogen‐bond acceptors, namely carbonyl groups, as well as one strong (NH) and one weak (C   sp   2–H) hydrogen‐bond donor. In addition to the hydrogen‐bonded sets of ester derivatives, acids 4 and 5 present the carboxylic acid moiety, which acts as both a hydrogen‐bond donor and acceptor. EDT‐TTF‐CO‐GlyOH has been previously used to afford a new type of hydrogen‐bonded acid/zwitterion (1:1) hybrid admixture of redox peptidics.