An artificial polypeptide receptor (APR) library was created by using the self-organization of N-lipidated
peptides attached to cellulose via m-aminophenylamino-1,3,5-triazine. The response of the library was probed using a
series of novel H3 receptor ligands. Since no guidelines on how to design an APRs selective vs certain receptor types
exist, a diverse set of amino acids (Ala, Trp, Pro, Glu, His, Lys and Ser) were used and coupled with one of three gating
fatty acids (palmitic, ricinoleic or capric). A competitive adsorption-desorption of an appropriate reporter dye was used
for the indirect visualization of the interactions of guests with particular receptors. The resulted library response to
individual inhibitors was then arranged in a matrix, preprocessed and analyzed using the principal component analysis
(PCA) and partial least squares (PLS) method. The most important conclusion obtained from the PCA analysis is that the
library differentiates the probed compounds according to the lipophilicity of the gating unit. The PC3 with a dominant
absolute contribution of the receptors containing Glu allowed for the best separation of the ligands with respect to their
activity. This conclusion is in agreement with the fact that Glu 206 is a genuine ligand counterpart in the natural histamine
Diagnostic platform, exploratory analysis, molecular recognition, peptide artificial receptor library, triazine.
Institute of Chemistry, University of Silesia, 40-006 Katowice, Poland.