Supramolecular organization of apolipoprotein A-I - derived peptides within disc-like arrangements

Apolipoprotein A-I is the major protein component of HDL and fulfils important functions in lipid metabolism. Its structure consists of a chain of tandem domains of amphipathic helices. Using this protein as a template membrane scaffolding proteins, class A amphipathic helical peptides were designed to support the amphipathic helix theory and later, as therapeutic tools in biomedicine. Here we investigated the lipid interactions of two apolipoprotein A-I derived class A amphipathic peptides, 14A (Ac-DYLKA FYDKL KEAF-NH2) and 18A (Ac-DWLKA FYDKV AEKLK EAF- NH2), including the disc-like supramolecular structures they form with phospholipids.

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