Biophysical Reviews

, Volume 11, Issue 3, pp 431–448 | Cite as

The role of membrane tension in the action of antimicrobial peptides and cell-penetrating peptides in biomembranes

  • Moynul Hasan
  • Md. Mizanur Rahman Moghal
  • Samiron Kumar Saha
  • Masahito YamazakiEmail author


For antimicrobial peptides (AMPs) with antimicrobial and bactericidal activities and cell-penetrating peptides (CPPs) with activity to permeate through plasma membrane, their interactions with lipid bilayer region in plasma membrane play important roles in these functions. However, the elementary processes and mechanisms of their functions have not been clear. The single giant unilamellar vesicle (GUV) method has revealed the details of elementary processes of interaction of some AMPs and CPPs with lipid vesicles. In this review, we summarize the mode of action of AMPs such as magainin 2 (Mag) and CPPs such as transportan 10 (TP10), revealed by the single GUV methods, and especially we focus on the role of membrane tension in actions of Mag and TP10 and the mechanisms of their actions. First, we explain the characteristics of the single GUV method briefly. Next, we summarize the recent view on the effect of tension on physical properties of lipid bilayers and describe the role of tension in actions of Mag and TP10. Some experimental results indicate that Mag-induced pore is a stretch-activated pore. The effect of packing of transbilayer asymmetric lipid on Mag-induced pore formation is described. On the other hand, entry of fluorescent dye, carboxyfluorescein (CF)-labeled TP10 (i.e., CF-TP10), into single GUVs without pore formation is affected by tension and high concentration of cholesterol. Pre-pore model for translocation of CF-TP10 across lipid bilayer is described. The experimental methods and their analysis described here are useful for investigation of functions of the other types of AMPs, CPPs, and proteins.


Single vesicles Giant unilamellar vesicles Pore formation Membrane permeation Pre-pores Asymmetric lipid packing 


Funding information

This work was supported in part by a Grant-in-Aid for Scientific Research (B) (No. 15H04361 and 19H03193) from the Japan Society for the Promotion of Science (JSPS) to M.Y.

Compliance with ethical standards

Conflict of interest

Moynul Hasan declares that he has no conflict of interest. Md. Mizanur Rahman Moghal declares that he has no conflict of interest. Samiron Kumar Saha declares that he has no conflict of interest. Masahito Yamazaki declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.


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© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Integrated Bioscience Section, Graduate School of Science and TechnologyShizuoka UniversityShizuokaJapan
  2. 2.Department of PharmacyJagannath UniversityDhakaBangladesh
  3. 3.Nanomaterials Research Division, Research Institute of ElectronicsShizuoka UniversityShizuokaJapan
  4. 4.Department of Physics, Faculty of ScienceShizuoka UniversityShizuokaJapan

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