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Amino Acid Derivatives of Tetrathiafulvalene and Their N–H···O Peptide Bond Dipoles‐Templated Solid State Assemblies
Author(s) -
ElGhayoury Abdelkrim,
Zorina Leokadiya,
Simonov Sergey,
Sanguinet Lionel,
Batail Patrick
Publication year - 2013
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201201330
Subject(s) - chemistry , hydrogen bond , tetrathiafulvalene , moiety , zwitterion , acceptor , stereochemistry , peptide , triple bond , amino acid , low barrier hydrogen bond , polymer chemistry , organic chemistry , molecule , double bond , biochemistry , physics , condensed matter physics
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.