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Staphylokinase Displays Surprisingly Low Mechanical Stability.

Chengzhi He¹, Hongbin Li¹

¹Department of Chemistry, University of British Columbia , Vancouver, BC V6T 1Z1, Canada.

Langmuir : the ACS Journal of Surfaces and Colloids

|January 3, 2017

Summary

Staphylokinase (SAK), a protein with a β-grasp fold, unexpectedly shows low mechanical stability. Its high malleability, not its structure, causes it to be the weakest known protein in its class.

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Area of Science:

Biophysics
Structural Biology
Protein Mechanics

Background:

Single-molecule force spectroscopy (SMFS) and molecular dynamics (MD) simulations identify shear topology as crucial for protein mechanical stability.
Proteins with a β-grasp fold typically exhibit shear topology and are mechanically robust.

Purpose of the Study:

To experimentally identify mechanically strong proteins using single-molecule atomic force microscopy.
To investigate the mechanical stability of staphylokinase (SAK) and its structural homologues.

Main Methods:

Single-molecule force spectroscopy (SMFS) using atomic force microscopy.
Molecular dynamics (MD) simulations (coarse-grained).

Main Results:

Staphylokinase (SAK) exhibits surprisingly low mechanical stability, unfolding at ~60 pN, making it the weakest known β-grasp protein.
In contrast, the homologous streptokinase β domain shows significant mechanical stability under identical conditions.
The native-state malleability of SAK is identified as the primary reason for its low mechanical stability.

Conclusions:

Protein mechanical stability is more complex than previously understood, with malleability playing a critical role.
The molecular basis for SAK's high malleability requires further investigation.
Detailed studies are needed to understand the molecular determinants of protein mechanical malleability.