Elucidation of the mechanisms of functions of antimicrobial peptides and cell-penetrating peptides using the single giant unilamellar vesicle (GUV) method

2017 Fiscal Year Final Research Report

• Project/Area Number: 15H04361
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biophysics
• Research Institution: Shizuoka University
• Principal Investigator: Yamazaki Masahito 静岡大学, 電子工学研究所, 教授 (70200665)
• Co-Investigator(Kenkyū-buntansha): 岡 俊彦 静岡大学, 電子工学研究所, 准教授 (60344389)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 一分子科学 / 生体膜 / 巨大リポソーム / 抗菌ペプチド / 膜透過ペプチド（細胞透過ペプチド） / ポア形成 / 膜透過 / 膜張力

Outline of Final Research Achievements

To elucidate the mechanisms of pore formation induced by antimicrobial peptides (AMPs) such as magainin 2 and entry of cell-penetrating peptides (CPPs) such as transportan 10 (TP10) into vesicle lumen, we investigated the effects of several factors such as membrane tension on these functions using the single giant unilamellar vesicle method. We found that a magainin 2-induced pore is a stretch-activated pore and constructed a quantitative model of the initial stage of magainin 2-induced pore formation. We found the effects of mechanical properties of lipid bilayer (such as tension and cholesterol) on entry of TP10 into single GUVs, and proposed a hypothesis on the mechanism of entry of TP10 across lipid bilayers. We also revealed the elementary processes of functions of other AMPs (lactoferricin B and lactoferricin B (4-9)) and CPPs (oligoarginine).

Free Research Field

生物物理学