IP Library Granted Patent US 9,234,029
Granted Patent B2
US 9,234,029 · App. 14/033,994 · Granted Jan 12, 2016

Stabilized fibronectin domain compositions, methods and uses

Inventor: Steven Jacobs (Spring House, PA)
Assignee: Janssen Biotech, Inc.
C07K14/78C12N15/1044A61K38/00
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 9,234,029
App. No.
14/033,994
Granted
Jan 12, 2016
Kind
B2
Abstract

A protein scaffold based on a consensus sequence of fibronectin type III (FN3) proteins, such as the tenth FN3 repeat from human fibronectin (human Tenascin), including isolated nucleic acids that encode a protein scaffold, vectors, host cells, and methods of making and using thereof, exhibit enhanced thermal and chemical stability while presenting six modifiable loop domains which can be engineered to form a binding partner capable of binding to a target for applications in diagnostic and/or therapeutic compositions, methods and devices.

Claims (5)

1. A protein scaffold comprising loop domains topologically similar to loop domains of a fibronectin type III (FN3) domain, the protein scaffold having an amino acid sequence based on the consensus amino acid sequence of SEQ ID NO: 16, wherein one or more specific residues of SEQ ID NO: 16 are replaced to enhance melting temperature (Tm) and chemical stability of the protein scaffold as compared to the Tm and chemical stability of a protein scaffold having the amino acid sequence of SEQ ID NO: 16, and the replacements of SEQ ID NO: 16 are selected from the group consisting of N46V, E14P, L17A, E86I, a combination of N46V and E86I, a combination of N46V and E86I, and a combination of L17A, N46V and E86I.

2. The protein scaffold of claim 1 , wherein the Tm is measured by differential scanning calorimetry, the chemical stability is measured as [D] by resistance to guanidinium chloride denaturation, and the Tm is increased as compared to the protein scaffold having the amino acid sequence of SEQ ID NO: 16 from about 1 Kcal to about 12 Kcal.

3. The protein scaffold of claim 1 , comprising loop regions for contacting a target protein, wherein the loop regions have been modified to encompass alternate residues to positions in the amino acid sequence of SEQ ID NOS: 16, and 142, 143 and 147-151 at one or more positions selected from the group consisting of residues 13, 15, and 16, 22-28, 38-43, 51-54, 60-64, and 75-81 of an amino acid sequence selected from the group consisting of SEQ ID NOS: 16, and 142, 143 and 147-151.

4. The protein scaffold of claim 3 , wherein said protein scaffold binds a target protein with at least one affinity selected from a K D of at least 10 −9 M, at least 10 −10 M, at least 10 −11 M, at least 10 −12 M, at least 10 −13 M, at least 10 −14 M, and at least 10 −15 M, as determined by surface plasmon resonance or the Kinexa method.

5. A protein scaffold comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 142-144 and 147-151.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 12, 2019
From: JACOBS, STEVEN
To: CENTOCOR ORTHO BIOTECH INC.
Reel/Frame 049735/0452 →
CHANGE OF NAME Recorded Jul 12, 2019
From: CENTOCOR ORTHO BIOTECH INC.
To: JANSSEN BIOTECH, INC.
Reel/Frame 049745/0466 →
Continuity (3)
Division 13097587 · Apr 29, 2011
Provisional Application 61329980 · Apr 30, 2010
Related Publication 20140018519A1 · Jan 16, 2014