Influence of a transmembrane domain on calcium-membrane interaction

author: Adela Melcrova, Academy of Sciences of the Czech Republic
published: July 9, 2018,   recorded: May 2018,   views: 364
Categories

Slides

Related Open Educational Resources

Related content

Report a problem or upload files

If you have found a problem with this lecture or would like to send us extra material, articles, exercises, etc., please use our ticket system to describe your request and upload the data.
Enter your e-mail into the 'Cc' field, and we will keep you updated with your request's status.
Lecture popularity: You need to login to cast your vote.
  Bibliography

Description

Calcium plays a significant role in various cellular processes including cell signaling or membrane fusion. Calcium ions have strong interactions with the negatively charged inner leaflet of plasma membrane (PM) where are the target molecules of many signaling pathways. Changes in biophysical properties of phospholipid membranes upon calcium binding were recently investigated (1). We took another step in further understanding the calcium binding to biologically relevant model of PM by incorporating a transmembrane peptide. We designed the peptide as a single transmembrane helix with either zero total charge or with a mild amount of positive charge. The positively charged peptide follows the so called positive-inside rule stating that the excess positive charge of helical TM proteins resides at the cytoplasmic side of the PM. The positive charge is however expected to repel the calcium ions. We use time-resolved emission spectroscopy of lipid vesicles accompanied by zeta potential measurements. The fluorescence technique gives us information on hydration and mobility of molecules in the vicinity of a fluorescent probe whereas the zeta potential shows trends in surface charge on the studied membranes. We found out that both transmembrane peptides indeed rigidify phospholipid bilayers. The positive charge only strenghtens this effect. Surprisingly, the positive charge of the peptide has no influence on calcium binding to membranes which is the same regardless the peptide content.

1. Melcrova et al. The complex nature of calcium cation interactions with phospholipid bilayers. Scientific Reports. 2016;6(1):38035. Available from: doi: 10.1038/srep38035.

Financing: Czech Science Foundation, Martina Roeselová Memorial Fellowship, Charles University project SVV

Link this page

Would you like to put a link to this lecture on your homepage?
Go ahead! Copy the HTML snippet !

Write your own review or comment:

make sure you have javascript enabled or clear this field: