Chromatographic characterisation of an estrogen-binding affinity column containing tetrapeptides selected by a combinatorial-binding approach.
In our work we performed a combinatorial synthesis in aqueous medium to prepare peptide libraries from which we would select amino acid sequences with binding properties towards estrogens. We prepared an affinity solid-phase by using a tetrapeptide with good selectivity and affinity towards the estradiol (K> 10(4) M(-1)). Samples of estrogens in buffer, in tap water and in river water were applied to our column in which they were retained (k' > 116). These could only be eluted in a few millilitres of methanol mobile phase. In all cases there were quantitative recoveries. The pre-concentration studies were promising.
Tozzi
Cinzia
C
Department of Analytical Chemistry, University of Torino, Turin, Italy. cinzia.tozzi@unito.it
Anfossi
Laura
L
Giraudi
Gianfranco
G
Giovannoli
Cristina
C
Baggiani
Claudio
C
Vanni
Adriano
A
D002846:Chromatography, Affinity / Q000379:methods*; D020650:Combinatorial Chemistry Techniques; D004797:Enzyme-Linked Immunosorbent Assay; D004967:Estrogens / Q000378:metabolism*; D009842:Oligopeptides / Q000737:chemistry*; D011485:Protein Binding
D004967:Estrogens; D009842:Oligopeptides