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Synthesis and Conformational Study of Monosubstituted Aminoferrocene‐Based Peptides Bearing Homo‐ and Heterochiral Pro‐Ala Sequences
Author(s) -
Čakić Semenčić Mojca,
Kodrin Ivan,
Barišić Lidija,
Nuskol Marko,
Meden Anton
Publication year - 2017
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201600648
Subject(s) - chemistry , chirality (physics) , hydrogen bond , conformational isomerism , intermolecular force , stereochemistry , ferrocene , molecule , amino acid , crystal structure , crystallography , computational chemistry , organic chemistry , biochemistry , physics , chiral symmetry breaking , electrode , quantum mechanics , nambu–jona lasinio model , electrochemistry , quark
The synthesis and conformational analysis of a series of the monosubstituted aminoferrocene‐based peptides bearing homo‐ and heterochiral Pro‐Ala sequences are described. A change of the Pro amino acid chirality can affect the secondary structure. The homochiral derivatives of t BuCO–AA 2 –AA 1 –NHFc (Fc = ferrocene; AA = Pro, Ala) favour β‐turns, and a disruption of the secondary structure is observed for the heterochiral analogues in solution. A detailed computational study suggested that γ‐turns form in the heterochiral derivatives. The X‐ray‐determined crystal structures of the heterochiral compounds show a preference for β‐turns. The calculated interaction energies indicate the significance of the intermolecular hydrogen bonds, which are favourable enough to overcome the rearrangement of a single molecule from the most stable conformer to that adopted in the solid state. The current research indicates the potential of the investigated compounds for the fine tuning of their conformational properties by variation of the chirality of the constituent amino acids.