Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene.

ABSTRACT: Engineered odorant-binding proteins (OBPs) display tunable binding affinities triggered by temperature alterations. We designed and produced two engineered proteins based on OBP-I sequence: truncated OBP (tOBP) and OBP::GQ₂₀::SP-DS3. The binding affinity of 1-aminoanthracene (1-AMA) to these proteins revealed that tOBP presents higher affinity at 25 °C (kd = 0.45 μM) than at 37 °C (kd = 1.72 μM). OBP::GQ₂₀::SP-DS3 showed an opposite behavior, revealing higher affinity at 37 °C (kd = 0.58 μM) than at 25 °C (kd = 1.17 μM). We set-up a system containing both proteins to evaluate their temperature-dependent binding. Our data proved the 1-AMA differential and reversible affinity towards OBPs, triggered by temperature changes. The variations of the binding pocket size with

SUBMITTER: Goncalves F 

PROVIDER: S-EPMC6172251 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature