Biophysical Reviews

, Volume 11, Issue 3, pp 419–430 | Cite as

Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature

  • Freda J. Passam
  • Joyce ChiuEmail author


Disulphide bonds are covalent linkages of two cysteine residues (R-S-S-R′) in proteins. Unlike peptide bonds, disulphide bonds are reversible in nature allowing cleaved bonds to reform. Disulphide bonds are important structural elements that stabilise protein conformation. They can be of catalytic function found in enzymes that facilitate redox reactions in the cleavage/formation of disulphide bonds in their substrates. Emerging evidence also indicates that disulphide bonds can be of regulatory function which alter protein activity when they are cleaved or formed. This class of regulatory disulphide bonds is known as allosteric disulphide bonds. Allosteric disulphide bonds are mechano-sensitive, and stretching or twisting the sulphur-sulphur bond by mechanical force can make it easier or harder to be cleaved. This makes allosteric disulphide bonds an ideal type of mechano-sensitive switches for regulating protein functions in the vasculature where cells are continuously subjected to fluid shear force. This review will discuss the chemistry and biophysical properties of allosteric disulphide bonds and how they emerge to be mechano-sensitive switches in regulating platelet function and clot formation.


Disulphide bonds Protein functions Vasculature 


Author contribution

JC wrote the review with FJP.

Compliance with ethical standards


Funding was provided by Helen and Robert Ellis Postdoctoral Fellowship from the Sydney Medical School Foundation (JC), and the National Health and Medical Research Council of Australia (FJP) and Sydney Cardiovascular Fellowship (FJP).

Conflict of interest

Freda J. Passam declares that she has no conflict of interest. Joyce Chiu declares that she 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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Copyright information

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

Authors and Affiliations

  1. 1.Heart Research Institute and Charles Perkins centreUniversity of SydneyCamperdownAustralia
  2. 2.The Centenary Institute, NHMRC Clinical Trial Centre, Sydney Medical SchoolUniversity of SydneyCamperdownAustralia

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