Engineering of a functional γ-tocopherol transfer protein.

ABSTRACT: α-tocopherol transfer protein (TTP) was previously reported to self-aggregate into 24-meric spheres (α-TTP_S) and to possess transcytotic potency across mono-layers of human umbilical vein endothelial cells (HUVECs). In this work, we describe the characterisation of a functional TTP variant with its vitamer selectivity shifted towards γ-tocopherol. The shift was obtained by introducing an alanine to leucine substitution into the substrate-binding pocket at position 156 through site directed mutagenesis. We report here the X-ray crystal structure of the γ-tocopherol specific particle (γ-TTP_S) at 2.24 Å resolution. γ-TTP_S features full functionality compared to its α-tocopherol specific parent including self-aggregation potency and transcytotic activity in tra

SUBMITTER: Aeschimann W 

PROVIDER: S-EPMC7677715 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature