Mdrna, Inc.

Marina Biotech, Inc.

Nastech Pharmaceutical Company, Inc.

Douglas L Badders

Richard E Herman

Steven C Quay

Michael E Houston, Jr

Paul Hickok Johnson

Mark Fuller

Ekaterina G Makienko

Trp cage binding domains polypeptides are disclosed. The Trp cage binding domains have the generic formulae of SEQ ID NO: 2, 7, 10 or 11. They can be efficiently produced and screened using phage display technology.

Phage displayed Trp cage ligands

This disclosure provides the construction, expression, and selection of the mutated genes that encode novel Trp cage polypeptides with desirable binding properties, as well as the novel Trp cage polypeptides themselves. The substances or targets bound by these novel Trp cage polypeptides may be but need not be proteins or polypeptides. Targets may include other biological or synthetic macromolecules as well as other organic and inorganic substances. Further, targets may also include a single or multiple cell or tissue types. The present invention achieves genetic variants of Trp cage-encoding nucleic acids through controlled random mutagenesis of the nucleic acids yielding a mixture of Trp cage polypeptides that are capable of binding targets.

Phage displayed cell binding peptides

The present disclosure relates to the construction, expression, and selection of genes that encode novel Trp cage polypeptides with desirable cell and/or tissue binding properties, as well as the novel Trp cage polypeptides themselves. A polypeptide of this disclosure may contain all or part of amino acid sequence AAADXYXQWLXXXGPXSGRPPPX(SEQ ID NO: 4), wherein Xrepresents an amino acid found in position n, the polypeptide comprising a tryptophan cage (Trp cage).

Trp cage binding domain polypeptides are disclosed. The Trp cage binding domains have the generic formulas of SEQ ID NO: 2, 7, 10 or 11. They can be efficiently produced and screened using phage display technology.

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Seattle, WA, United States of America

Douglas L Badders