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.
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