Substrate specificity of an actively assembling amyloid catalyst

J.L. Heier, D.J. Mikolajczak, C. Böttcher, B. Koksch – 2017

In the presence of Zn2+ , the catalytic, amyloid-forming peptide Ac-IHIHIQI-NH2 , was found to exhibit enhanced selectivity for hydrophobic p-nitrophenyl ester substrates while in the process of self-assembly. As opposed to the substrate p-nitrophenyl acetate, which was more effectively hydrolyzed with Ac-IHIHIQI-NH2 in its fully fibrillar state, the hydrophobic substrate Z-L-Phe-ONp was converted with a second-order rate constant more than 11-times greater when the catalyst was actively assembling. Under such conditions, Z-L-Phe-ONp hydrolysis proceeded at a greater velocity than the more hydrophilic and otherwise more labile ester Boc-L-Asn-ONp. When assembling, the catalyst also showed increased selectivity for the L-enantiomer of Z-Phe-ONp. These findings suggest the occurrence of increased interactions of hydrophobic moieties of the substrate with exposed hydrophobic surfaces of the assembling peptides and present valuable features for future de novo design consideration.

Titel
Substrate specificity of an actively assembling amyloid catalyst
Verfasser
J.L. Heier, D.J. Mikolajczak, C. Böttcher, B. Koksch
Datum
2017
Kennung
10.1002/bip.23003.
Zitierweise
Biopolymers 2017, 108, e23003
Art
Text
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