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Flat, Ferrocenyl‐Conjugated Peptides: A Combined Electrochemical and Spectroscopic Study
Author(s) -
Biondi Barbara,
Cardena Roberta,
Bisello Annalisa,
Schiesari Renato,
Cerveson Laura,
Facci Martino,
Rancan Marzio,
Formaggio Fernando,
Santi Saverio
Publication year - 2021
Publication title -
chemelectrochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.182
H-Index - 59
ISSN - 2196-0216
DOI - 10.1002/celc.202100597
Subject(s) - peptide , conjugated system , moiety , ferrocene , chemistry , residue (chemistry) , cyclic voltammetry , electrochemistry , helix (gastropod) , conjugate , dipole , stereochemistry , crystallography , combinatorial chemistry , organic chemistry , electrode , biochemistry , polymer , ecology , mathematical analysis , mathematics , snail , biology
Abstract We synthesized two homo‐peptide series, based on the C α,β ‐didehydroalanine residue. One series was functionalized with a ferrocene (Fc) moiety at the N‐terminus, the other series with a Fc at the C‐terminus. These conjugates adopt the flat, fully extended conformation, also known as 2.0 5 ‐helix. Cyclic voltammetry measurements revealed that the peptide length does not affect the redox behavior of Fc, independently on the peptide end at which it is appended. This outcome perfectly fits with the presence of fully‐extended peptides, as in this 3D‐structure the dipole moment is negligible. Thus, we confirm the results of our previous study with two Fc pendants: fully‐extended, α‐peptide stretches prevent or reduce the charge transfer along the peptide chain.