Notice of RetractionIn Silico Investigation of Interaction between Human Neutrophil Elastase and Sea Anemone Heteractis crispa Kunitz Polypeptides

Notice of Retraction

After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.

We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.

The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.

Serine proteinase neutrophil elastase plays a principle role in inflammatory processes. Therefore, explanation of the selective elastase inhibitors action mechanisms attracts the great interest of the modern biomedicine and bioinformatics. Currently, there are many investigations devoted to search of polypeptide agents effectively suppressing the inflammatory process. Recent studies have shown that some Kunitz type serine proteinase inhibitors may render an anti-inflammatory effect. Here we represent model of complexes of sea anemone Heteractis crispa Kunitz polypeptides (HCPs) with human neutrophil elastase (HNE) and discuss driving forces of the enzyme-inhibitor interaction. Proposed models allow for the first time to clarify the molecular mechanism of these polypeptides anti-inflammatory action.