Fragments of Locusta migratoria apoLp-III provide insight into lipid binding.

ABSTRACT: Apolipophorin III (apoLp-III) from Locusta migratoria is an exchangeable apolipoprotein with a critical role in lipid transport in insects. The protein is composed of a bundle of five amphipathic α-helices which undergo a large conformational change upon lipid binding. To better understand the apoLp-III lipid binding interaction, the protein was cleaved by cyanogen bromide upon introduction of a S92M mutation, generating an N-terminal fragment corresponding to the first three helices (NT_H1-3) and a C-terminal fragment of the last two helices (CT_H4-5). MALDI-TOF analysis of the HPLC purified fragments provided masses of 9863.8 Da for NT_H1-3 and 7497.0 Da for CT_H4-5 demonstrating that the intended fragments were obtained. Circular dichroism

SUBMITTER: Russell BA 

PROVIDER: S-EPMC9581338 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature