Biochemistry: Molecular cloaking devices

Nature (Impact Factor: 41.46). 07/2008; 453(7197):861-2. DOI: 10.1038/453861a
Source: PubMed


Protease enzymes cut other proteins into pieces, but some can be blocked by inhibitors. One such inhibitor binds to the substrate rather than the enzyme, suggesting a new tactic for drug discovery.

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    • "Over-manifestation of the cellular protease is the kernel factor for genesis of various human body disorders. The development mechanism of a protease and their proteolysis of specific peptide (or protein) as substrate have played a pivotal role on genesis of inflammatory disease and outbreaks of cancer and their metastasis by sudden change of physiological condition and immune system [1]. Recently, synthetic polymers conjugated to drug (or specific molecules) via peptide linker chain have been employed as a targeted drug carrier [2]–[4]. "
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    ABSTRACT: Characterization and control of proteolysis of peptides by specific cellular protease is a priori requisite for effective drug discovery. Here, we report the nanomechanical, in situ monitoring of proteolysis of peptide chain attributed to protease (Cathepsin B) by using a resonant nanomechanical microcantilever immersed in a liquid. Specifically, the detection is based on measurement of resonant frequency shift arising from proteolysis of peptides (leading to decrease of cantilever's overall mass, and consequently, increases in the resonance). It is shown that resonant microcantilever enables the quantification of proteolysis efficacy with respect to protease concentration. Remarkably, the nanomechanical, in situ monitoring of proteolysis allows us to gain insight into the kinetics of proteolysis of peptides, which is well depicted by Langmuir kinetic model. This implies that nanomechanical biosensor enables the characterization of specific cellular protease such as its kinetics.
    PLoS ONE 02/2009; 4(7):e6248. DOI:10.1371/journal.pone.0006248 · 3.23 Impact Factor

  • Nature Reviews Drug Discovery 08/2008; 7(8):646-646. DOI:10.1038/nrd2646 · 41.91 Impact Factor
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    ABSTRACT: Viele Enzymaktivitäten lassen sich durch Effektoren regulieren, die an das katalytische Zentrum oder ein allosterisches Zentrum des Enzyms binden. Jetzt kamen Wissenschaftler einem neuartigen Typ von Proteaseinhibitoren auf die Spur, die spezifisch an Proteinsubstrate binden und so deren proteolytische Spaltung hemmen.
    Chemie in unserer Zeit 10/2008; 42(5):306-306. DOI:10.1002/ciuz.200890056 · 0.26 Impact Factor
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