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Interactions of ferrocenoyl‐peptides in solution and on surfaces
Author(s) -
Kraatz HeinzBernhard
Publication year - 2003
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200390174
Subject(s) - cystamine , ferrocene , supramolecular chemistry , alanine , peptide , glycine , conjugate , hydrogen bond , chemistry , monolayer , self assembled monolayer , electrochemistry , intermolecular force , stereochemistry , combinatorial chemistry , materials science , crystallography , molecule , amino acid , organic chemistry , biochemistry , crystal structure , electrode , mathematical analysis , mathematics
The Ferrocenoyl‐peptide‐cystamines, such as [Fc‐Gly‐CSA] 2 (Gly = glycine, CSA = cystamine), [Fc‐Ala‐CSA] 2 (Ala = alanine) and Fc‐conjugates involving collagen models, such as [Fc‐(Pro 2 Gly) n ‐CSA] 2 (Pro = proline, n = 1‐6) are readily prepared by solution methods. In solution and the solid state, these systems exhibit intermolecular hydrogen bonding between adjacent peptide chains. For [Fc‐Gly‐CSA] 2 this results in the formation of a supramolecular helicate with two different H‐bonding patterns. Ferrocenoyl‐collagen‐cystamines form assemblies in solution, which melt at elevated tempertures. All systems for monolayers on gold surfaces, which show a well‐behaved ferrocene‐based electrochemistry, which allows the determination of the spatial requirements of the peptides on the surface.