Structural change and interaction analysis of antimicrobial peptides in membrane conditions

2016 Fiscal Year Final Research Report

• Project/Area Number: 26440072
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Hokkaido University
• Principal Investigator: AIZAWA TOMOYASU 北海道大学, 先端生命科学研究院, 准教授 (40333596)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: ペプチド / 抗菌ペプチド / 遺伝子組換え / NMR / LPS / 大腸菌 / 酵母

Outline of Final Research Achievements

Antimicrobial peptides are considered an essential part of the innate immune response of plants, invertebrates and vertebrates as they provide host defenses and can target a wide range of pathogenic microorganisms, including bacteria, fungi, yeast, parasites and viruses. Antimicrobial peptides are thought to kill bacteria by breaking their cell membranes, although the exact mechanisms are still unclear. In this study, we investigated efficient way to prepare isotopically labelled antimicrobial peptides for NMR studies. By using an isotopically labelled antimicrobial peptide, we obtained structural information for LPS-bound form.

Free Research Field

蛋白質科学