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Designer Peptides: Attempt to Control Peptide Structure by Exploiting Ferrocene as a Scaffold
Author(s) -
Lataifeh Anas,
Beheshti Samaneh,
Kraatz HeinzBernhard
Publication year - 2009
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.200900268
Subject(s) - chemistry , ferrocene , intramolecular force , scaffold , supramolecular chemistry , peptide , hydrogen bond , conjugate , intermolecular force , combinatorial chemistry , molecule , stereochemistry , nanotechnology , electrochemistry , biochemistry , organic chemistry , materials science , electrode , medicine , mathematical analysis , mathematics , biomedical engineering
The design of peptides that display a β‐sheet‐like secondary structure remains a challenge. Molecular scaffolds, such as ferrocene (Fc) can help to overcome some of these challenges. Monosubstituted Fc derivatives offer no control over the self‐assembly of the conjugates, and the formation of supramolecular structures is entirely serendipitous. 1, n′ ‐disubstituted Fc derivatives provide a significant level of control over the direction of the peptide, their relative orientation, and the intramolecular hydrogen‐bonding patterns, which increases the rigidity of the molecule and in many cases, generates a new H‐bonding interface for intermolecular assembly. In this Microreview, we explore the use of ferrocene as a scaffold in the design of structurally well‐defined peptide conjugates. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)