Jefferson Susan L Foote from 4103 Sunnyside Ave N, Seattle, WA 98103, Phone: 2065475939

Resumes

Jefferson Foote

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Location:

Seattle, WA

Industry:

Biotechnology

Work:

Arrowsmith Technologies - Seattle, WA since 2006
Co-founder and Chief Science Officer
Absalus, Inc. - Silicon Valley; Australia 2004 - 2004
Co-founder
Fred Hutchinson Cancer Research Center; University of Washington - Seattle, WA 1992 - 2004
Faculty, Division of Molecular Medicine; Co-appointment at UW in Immunology, Biomolecular Structure

Education:

MRC Laboratory of Molecular Biology 1985 - 1992
Postdoctoral and staff positions, Antibody engineering and biophysical chemistry University of California, Berkeley 1980 - 1985
PhD, Biochemistry Harvard University 1973 - 1977
AB, Biochemical Sciences

Skills:

Immunology
Patents
Biotechnology
Antibodies
Biophysics
Science
In Vivo
Molecular Biology
Pharmaceutical Industry
Biochemistry
Drug Discovery
Protein Chemistry
Cell Biology
Protein Expression
Genomics

Us Patents

Method Of Humanizing Antibodies By Matching Canonical Structure Types Cdrs
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US Patent:

7709226, May 4, 2010
Filed:

May 10, 2006
Appl. No.:

11/432734
Inventors:

Jefferson Foote - Seattle WA, US
Assignee:

Arrowsmith Technology Licensing LLC - Seattle WA
International Classification:

C12P 21/04
C12N 5/06
C12P 21/06
C07K 16/00
C12P 21/08
US Classification:

435 696, 435 691, 435326, 435328, 5303871, 5303873, 5303881, 4241331, 4241411
Abstract:

Disclosed herein are methods for humanizing antibodies based on selecting variable region framework sequences from human antibody genes by comparing canonical CDR structure types for CDR sequences of the variable region of a non-human antibody to canonical CDR structure types for corresponding CDRs from a library of human antibody sequences, preferably germline antibody gene segments. Human antibody variable regions having similar canonical CDR structure types to the non-human CDRs form a subset of member human antibody sequences from which to select human framework sequences. The subset members may be further ranked by amino acid similarity between the human and the non-human CDR sequences. Top ranking human sequences are selected to provide the framework sequences for constructing a chimeric antibody that functionally replaces human CDR sequences with the non-human CDR counterparts using the selected subset member human frameworks, thereby providing a humanized antibody of high affinity and low immunogenicity without need for comparing framework sequences between the non-human and human antibodies. Chimeric antibodies made according to the method are also disclosed.

Super Humanized Antibodies
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US Patent:

7732578, Jun 8, 2010
Filed:

Feb 8, 2005
Appl. No.:

11/054669
Inventors:

Jefferson Foote - Seattle WA, US
Assignee:

Arrowsmith Technology Licensing LLC - Seattle WA
International Classification:

C07K 16/00
A61K 39/395
C12P 21/04
C12P 21/06
C12N 5/06
C07H 21/04
US Classification:

5303873, 4241331, 4241411, 4241541, 4241561, 435 691, 435 696, 435326, 435328, 5303871, 5303881, 53038875, 53038885
Abstract:

Disclosed herein are methods for humanizing antibodies based on selecting variable region framework sequences from human antibody genes by comparing canonical CDR structure types for CDR sequences of the variable region of a non-human antibody to canonical CDR structure types for corresponding CDRs from a library of human antibody sequences, preferably germline antibody gene segments. Human antibody variable regions having similar canonical CDR structure types to the non-human CDRs form a subset of member human antibody sequences from which to select human framework sequences. The subset members may be further ranked by amino acid similarity between the human and the non-human CDR sequences. Top ranking human sequences are selected to provide the framework sequences for constructing a chimeric antibody that functionally replaces human CDR sequences with the non-human CDR counterparts using the selected subset member human frameworks, thereby providing a humanized antibody of high affinity and low immunogenicity without need for comparing framework sequences between the non-human and human antibodies. Chimeric antibodies made according to the method are also disclosed.

Super Humanized Antibodies
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US Patent:

20030039649, Feb 27, 2003
Filed:

Jul 12, 2002
Appl. No.:

10/194975
Inventors:

Jefferson Foote - Seattle WA, US
International Classification:

G01N033/53
G06G007/48
G06G007/58
G06F019/00
G01N033/48
G01N033/50
A61K039/395
US Classification:

424/141100, 702/019000, 703/011000, 435/007100
Abstract:

Disclosed herein are methods for humanizing antibodies based on selecting variable region framework sequences from human antibody genes by comparing canonical CDR structure types for CDR sequences of the variable region of a non-human antibody to canonical CDR structure types for corresponding CDRs from a library of human antibody sequences, preferably germline antibody gene segments. Human antibody variable regions having similar canonical CDR structure types to the non-human CDRs form a subset of member human antibody sequences from which to select human framework sequences. The subset members may be further ranked by amino acid similarity between the human and the non-human CDR sequences. Top ranking human sequences are selected to provide the framework sequences for constructing a chimeric antibody that functionally replaces human CDR sequences with the non-human CDR counterparts using the selected subset member human frameworks, thereby providing a humanized antibody of high affinity and low immunogenicity without need for comparing framework sequences between the non-human and human antibodies. Chimeric antibodies made according to the method are also disclosed.

Antibody Buffering Of A Ligand In Vivo
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US Patent:

20060062778, Mar 23, 2006
Filed:

Sep 13, 2005
Appl. No.:

11/226055
Inventors:

Jefferson Foote - Seattle WA, US
Carol O'Hear - Seattle WA, US
International Classification:

A61K 39/395
US Classification:

424130100
Abstract:

Compositions and methods are provided in embodiments directed to maintaining a desired concentration range of one or more drugs in a subject, and in particular embodiments to maintaining a desired drug concentration in a body compartment in a subject, based on the surprising discovery that antibodies persist in solution in body compartments such that antibody-antigen equilibrium principles can counteract drug clearance mechanisms. One or more antibodies are selected that have a dissociation constant Kthat is similar to the desired drug concentration, wherein Kis independent of the affinity of the drug for a specific drug target (receptor) in the subject.

Super Humanized Antibodies
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US Patent:

20110137014, Jun 9, 2011
Filed:

Mar 29, 2010
Appl. No.:

12/749257
Inventors:

Jefferson Foote - Seattle WA, US
Assignee:

Arrowsmith Technology Licensing, LLC - Seattle WA
International Classification:

C07K 16/28
US Classification:

5303873
Abstract:

Disclosed herein are methods for humanizing antibodies based on selecting variable region framework sequences from human antibody genes by comparing canonical CDR structure types for CDR sequences of the variable region of a non-human antibody to canonical CDR structure types for corresponding CDRs from a library of human antibody sequences, preferably germline antibody gene segments. Human antibody variable regions having similar canonical CDR structure types to the non-human CDRs form a subset of member human antibody sequences from which to select human framework sequences. The subset members may be further ranked by amino acid similarity between the human and the non-human CDR sequences. Top ranking human sequences are selected to provide the framework sequences for constructing a chimeric antibody that functionally replaces human CDR sequences with the non-human CDR counterparts using the selected subset member human frameworks, thereby providing a humanized antibody of high affinity and low immunogenicity without need for comparing framework sequences between the non-human and human antibodies. Chimeric antibodies made according to the method are also disclosed.