Hostname: page-component-848d4c4894-r5zm4 Total loading time: 0 Render date: 2024-07-07T07:29:03.474Z Has data issue: false hasContentIssue false

Real-Time Observation of Phospholipid Bilayer Membrane Restructuring Induced by Protein Molecules using Atomic Force Microscopy

Published online by Cambridge University Press:  02 July 2020

Hong Xing You
Affiliation:
Department of Cell Biology, Neurobiology, and Anatomy, University of Cincinnati College of Medicine, 3125 Eden Ave, Cincinnati, OH, 45267-0521, USA
Xiaoyang Qi
Affiliation:
The Division of Human Genetics, Children’s Hospital Research Foundation, 3333 Burnet Ave, Cincinnati, OH, 45229-3039, USA
Lei Yu
Affiliation:
Department of Cell Biology, Neurobiology, and Anatomy, University of Cincinnati College of Medicine, 3125 Eden Ave, Cincinnati, OH, 45267-0521, USA
Get access

Abstract

Atomic force microscopy (AFM) allows the surfaces of native biological materials to be imaged in aqueous solution with submolecular resolution. The ability to perform AFM imaging in aqueous and physiological environment has made it possible to monitor important biological processes in real time at high resolution. Currently, there is a great deal of interest in AFM studies of the structure and property of lipid bilayer membranes and protein interactions with lipid bilayer membranes. Lipid bilayer membranes in biological cells form a permeability barrier, which controls the flow of ions, water, and other molecules between biological cells and their environments, whereas membrane-bound and/or membrane-associated proteins are responsible for most of the dynamic functions carried out by the membrane. However, real-time AFM monitoring of dynamic biological processes has been challenged by the limited temporal resolution of AFM, potential physical damage to soft biological samples, and intrinsic complexity of biological processes. There are few successful examples of AFM real-time studies of dynamic biological events, particularly in the aspect of protein interactions with lipid bilayer membranes.

We have attempted to use atomic force microscopy to study interactions between a particular protein, saposin C, and phospholipid bilayer membranes in real time. Saposin C (Sap C), a small glycoprotein, is an essential co-factor for the hydrolysis of glucosylceramide by glucosylceramidase in lysosomes, and a deficiency of Sap C leads to a variant form of Gauchers’ diseases. Supported planar phospholipid bilayer membranes were used in the study.

Type
Can Scanning Probe Microscopes Do Microanalysis? (Organized by I. Holl Musselman)
Copyright
Copyright © Microscopy Society of America 2001

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

references

1.Lai, R. and John, S. A.. Am. J. Physiol. 266 (1994) C1.Google Scholar
2.Shao, Z. and Yang, J.. Q. Rev. Biophys. 28 (1995) 195.CrossRefGoogle Scholar
3.You, H.X. and Yu, L.. Methods Cell Sci. 21 (1999) 1.CrossRefGoogle Scholar
4.Grandbois, M., Clausen-Schaumann, H. and Gaub, H.. Biophys. J. 14 (1998) 2398.CrossRefGoogle Scholar