Gold nanoparticles partition to and increase the activity of glucose-6-phosphatase in a synthetic phospholipid membrane system.

ABSTRACT: Engineered nanomaterials can alter the structure and/or function of biological membranes and membrane proteins but the underlying mechanisms remain unclear. We addressed this using a Langmuir phospholipid monolayer containing an active transmembrane protein, glucose-6-phosphatase (G6Pase). Gold nanoparticles (nAu) with varying ligand shell composition and hydrophobicity were synthesized, and their partitioning in the membrane and effects on protein activity characterized. nAu incorporation did not alter the macroscopic properties of the membrane. Atomic force microscopy showed that when co-spread with other components prior to membrane compression, nAu preferentially interacted with G6Pase and each other in a functional group-dependent manner. Under these conditions, all nAu formulations r

SUBMITTER: MacCormack TJ 

PROVIDER: S-EPMC5560555 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature