Yasser Bustanji and Bruno Samorì.

The mechanical properties of human Angiostatin can be modulated by means of its disulfide bonds: A Single-Molecule Force- Spectroscopy Study.

 

Angew. Chem .Int. Ed. 2002 ,41, 1546.

 

Human angiostatin 1-5 [Ang(1-5)], a 57 kDa proteolitic fragment of human plasminogen, consists of five compact globular modules called Kringle domains with very similar gross architecture and remarkable sequence homology. They are built around a hydrophobic core and exhibit a triple-loop topology defined by three internal disulfide bonds: cys 1-cys 80 (1), cys 22-cys 63 (2), and cys 51-cys 75 (3) Here we report on a single-molecule force-spectroscopy study that shows how the redox environment can control the topology and mechanical properties of angiostatin by modifying the extent of pairing of the internal disulfide bonds.