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Updated: Mar 12, 2026
08:38
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
Published on: March 3, 2015
14.0K
Strings and stripes formed by a protein system interacting via a single-patch attraction.
Weimin Li1, Maxim Morin1, Emil Gustafsson1
1Division of Physical Chemistry, Lund University, POB 124, 22100 Lund, Sweden. malin.zackrisson@fkem1.lu.se.
Soft Matter
|November 8, 2016
Summary
Lactoferrin self-assembles into unique stripe structures at specific concentrations due to directional attraction. These structures, difficult to detect conventionally, were visualized using advanced scattering and imaging techniques.
Area of Science:
- Biophysics
- Materials Science
- Protein Chemistry
Background:
- Proteins interact via various forces, influencing their solution behavior.
- Directional attractions, unlike isotropic ones, can lead to complex self-assembly.
- Lactoferrin exhibits patch-patch attraction under specific conditions.
Purpose of the Study:
- To investigate the phase behavior of lactoferrin.
- To understand self-assembly driven by directional protein-protein interactions.
- To characterize the formation of novel supramolecular structures.
Main Methods:
- Studying lactoferrin phase behavior as a function of concentration.
- Utilizing static light scattering to monitor protein concentration changes.
- Employing cryo-transmission electron microscopy (cryo-TEM) for structural visualization.
Main Results:
- Lactoferrin dimerizes at low concentrations.
- Elongated, stripe-like structures form at intermediate concentrations.
- These stripe phases are challenging to detect with traditional methods like small-angle X-ray scattering.
Conclusions:
- Directional attraction in lactoferrin leads to unique stripe-like self-assembly.
- Advanced techniques are necessary to observe these structures due to their low participation and sedimentation.
- The findings provide insights into protein self-organization driven by specific attractive forces.
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