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Selective Binding of Inhibitor‐Assisted Surface‐Imprinted Core/Shell Microbeads in Protein Mixtures
Author(s) -
Dinc Mehmet,
Basan Hasan,
Hummel Tim,
Müller Marlen,
Sobek Harald,
Rapp Ingrid,
Diemant Thomas,
Behm Rolf Jürgen,
Lindén Mika,
Mizaikoff Boris
Publication year - 2018
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201800129
Subject(s) - imprinting (psychology) , molecular imprinting , molecularly imprinted polymer , chemistry , chromatography , selectivity , solid phase extraction , chemical engineering , organic chemistry , extraction (chemistry) , biochemistry , catalysis , gene , engineering
An innovative approach for molecularly imprinting proteins, i. e., inhibitor‐assisted imprinting was used for addressing the major challenge of protein purification from biotechnologically relevant media. Pepstatin‐assisted pepsin surface‐imprinted microbeads were synthesized as a selective sorbent for solid phase extraction (SPE). The amino‐functionalized porous core was prepared by co‐condensation and post‐grafting strategies. The immobilized inhibitor pre‐organizes the template pepsin with a defined orientation prior to imprinting ensuring enhanced efficiency of the imprinting process. 3‐aminophenylboronic acid (APBA) was used as a functional monomer establishing organic nanoscale films comprising poly(3‐aminophenylboronic acid) (pAPBA) within the pores of the beads in the presence (MIP) and absence (NIP) of pepsin. Next to a detailed characterization of these advanced functional hybrid materials it was demonstrated that such porous surface‐imprinted core/shell beads feature exquisite selectivity for pepsin during individual protein rebinding studies, and more importantly, during competitive rebinding studies in protein mixtures.