Current Pharmaceutical Biotechnology

Zeno Foldes-Papp
Visiting Professor of Medical Biochemistry
HELIOS Clinical Center of Emergency Medicine
Department for Internal Medicine
Alte-Koelner-Strasse 9
D-51688 Koeln-Wipperfuerth
Germany

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A Novel Biological Actions Acquired by Ribonuclease Through Oligomerization

Author(s): M. Libonati, G. Gotte, F. Vottariello.

Abstract:

After a short introduction with some examples of cytotoxic ribonucleases, the importance of natural or artificial dimerization (oligomerization) as a way for a ribonuclease to acquire novel functional properties has been pointed out. In particular, the role of the three dimensional domain swapping mechanism in bovine pancreatic ribonuclease A oligomerization, as well as its impact for the acquisition of novel biological functions (among which a remarkable antitumor action) by the enzyme protein in oligomeric form have been discussed. Finally, the structural and functional features that could explain why oligomeric ribonuclease A becomes able to display a cytotoxic activity, and the possible use and limits of the three dimensional domain-swapped oligomers of ribonuclease A as anticancer therapeutic agents have been described and discussed.

Keywords: RNase A, RNase A dimers, RNase A oligomers, Cytotoxicity, RNase cytotoxicity, Cytotoxicity of oligomeric RNase A, Antitumor therapy, 3D domain swapping

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Article Details

VOLUME: 9
ISSUE: 3
Year: 2008
Page: [200 - 209]
Pages: 10
DOI: 10.2174/138920108784567308
Price: $58