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Aggregation Behavior of Giant Amphiphiles Prepared by Cofactor Reconstitution
Author(s) -
Boerakker Mark J.,
Botterhuis Nicole E.,
Bomans Paul H. H.,
Frederik Peter M.,
Meijer Emmo M.,
Nolte Roeland J. M.,
Sommerdijk Nico A. J. M.
Publication year - 2006
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200600089
Subject(s) - amphiphile , chemistry , cofactor , biophysics , biochemistry , organic chemistry , biology , polymer , copolymer , enzyme
We report on biohybrid surfactants, termed “giant amphiphiles”, in which a protein or an enzyme acts as the polar head group and a synthetic polymer as the apolar tail. It is demonstrated that the modification of horseradish peroxidase (HRP) and myoglobin (Mb) with an apolar polymer chain through the cofactor reconstitution method yields giant amphiphiles that form spherical aggregates (vesicles) in aqueous solution. Both HRP and Mb retain their original functionality when modified with a single polystyrene chain, but reconstitution has an effect on their activities. In the case of HRP the enzymatic activity decreases and for Mb the stability of the dioxygen myoglobin (oxy‐Mb) complex is reduced, which is probably the result of a disturbed binding of the heme in the apo‐protein or a reduced access of the substrate to the active site of the enzyme or protein.