NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs

Biophysical Journal
Ji-Ho JeongYongae Kim

Abstract

Lactophoricin (LPcin), a component of proteose peptone (113-135) isolated from bovine milk, is a cationic amphipathic antimicrobial peptide consisting of 23 amino acids. We designed a series of N- or C-terminal truncated variants, mutated analogs, and truncated mutated analogs using peptide-engineering techniques. Then, we selected three LPcin analogs of LPcin-C8 (LPcin-YK1), LPcin-T2WT6W (LPcin-YK2), and LPcin-T2WT6W-C8 (LPcin-YK3), which may have better antimicrobial activities than LPcin, and successfully expressed them in E. coli with high yield. We elucidated the 3D structures and topologies of the three LPcin analogs in membrane environments by conducting NMR structural studies. We investigated the purity of the LPcin analogs and the α-helical secondary structures by performing (1)H-(15)N 2D HSQC and HMQC-NOESY liquid-state NMR spectroscopy using protein-containing micelle samples. We measured the 3D structures and tilt angles in membranes by conducting (15)N 1D and 2D (1)H-(15)N SAMMY type solid-state NMR spectroscopy with an 800 MHz in-house-built (1)H-(15)N double-resonance solid-state NMR probe with a strip-shield coil, using protein-containing large bicelle samples aligned and confirmed by molecular-dynamics simulati...Continue Reading

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Citations

Oct 21, 2016·Biophysical Journal·Aritreyee DattaAnirban Bhunia
Aug 24, 2018·Biomolecules·Fatma Gizem AvciElif Ozkirimli
Mar 7, 2017·Frontiers in Neuroscience·Jianguo LiRoger W Beuerman
Jun 6, 2019·Pharmaceuticals·Boris VishnepolskyMalak Pirtskhalava
Jun 25, 2021·Journal of Chemical Information and Modeling·Pietro G A AronicaChandra S Verma
Sep 2, 2020·Biochimica Et Biophysica Acta. Biomembranes·Ji-Ho JeongYongae Kim

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