Concept

Kunitz domain

Related publications (6)

Bicyclic Peptide inhibitor reveals large contact interface with a protease target

Christian Heinis, Alessandro Angelini, Shiyu Chen, Jeremy Touati

From a large combinatorial library of chemically constrained bicyclic peptides we isolated a selective and potent (K(i) = 53 nM) inhibitor of human urokinase-type plasminogen activator (uPA) and crystallized the complex. This revealed an extended structure ...

2012

Measuring net protease activities in biological samples using selective peptidic inhibitors

Christian Heinis, Alessandro Angelini, Philippe Diderich, Lisa Pollaro, Silvia Bellotto, Hermann A. Wegner

The measurement of activities from individual proteases in biological samples is difficult because of the numerous proteases, their overlapping activities, and the lack of specific substrates. We applied selective protease inhibitors based on bicyclic pept ...

2012

Engineered aprotinin for improved stability of fibrin biomaterials

Peter Frey, Stephane Kontos, Jeffrey Alan Hubbell, Kristen Lorentz

Fibrin has been long used clinically for hemostasis and sealing, yet extension of use in other applications has been limited due to its relatively rapid resorption in vivo, even with addition of aprotinin or other protease inhibitors. We report an engineer ...

2011

Biofunctional Scaffold Design for Soft Tissue Regeneration

Kristen Lorentz

Fibrin has long been used clinically for hemostasis and sealing and has been extensively characterized as a biomaterial. Yet, in terms of harnessing its potential for use in tissue regeneration, there remains a wide gap between in vitro experimentation and ...

EPFL2011

Multi-scale modeling of HIV-1 proteins

Marilisa Neri, Paolo Carloni

The efficiency of protease inhibiting drugs is hampered by the rapid emergence of protease variants. Understanding this phenomenon requires the characterization of the salient steps of HIV-1 protease's catalytic cycle. We summarize Our investigations on th ...

2009

Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation

Françoise Gisou van der Goot Grunberg

The channel-forming protein aerolysin is secreted as a protoxin which can be activated by proteolytic removal of a C-terminal peptide. The activation and subsequent oligomerization of aerolysin were studied using a variety of spectroscopic techniques. Mass ...

1992

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