IP Library Granted Patent US 10,927,368
Granted Patent B2
US 10,927,368 · App. 15/886,271 · Granted Feb 23, 2021

Library-based methods and compositions for introducing molecular switch functionality into protein affinity reagents

Inventor: James R. Horn (Sycamore, IL)
Assignee: NORTHERN ILLINOIS RESEARCH FOUNDATION
C12N15/1037C07K16/40C07K16/44G01N33/6854C07K2317/14C07K2317/22C07K2317/569C07K2317/90C07K2317/92C40B30/04
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Quick Facts
Patent No.
US 10,927,368
App. No.
15/886,271
Granted
Feb 23, 2021
Kind
B2
Abstract

Methods and compositions are disclosed for introducing molecular switch functionality into a protein affinity reagent to render its binding to a target molecule sensitive to an environmental trigger, such as pH, while maintaining binding affinity to the target molecule. Combinatorial libraries created by the method are also disclosed.

Claims (13)

1. A method of selecting protein affinity reagents encoded by a synthetic combinatorial nucleic acid library, wherein the protein affinity reagents comprise a heavy chain variable domain antibody (VHH), wherein protein affinity reagents are selected that have molecular switch functionality sensitive to an environmental trigger, have a target binding interface, with a plurality of ionizable amino acid residues and wherein a specific target molecule is released from the protein affinity reagent in the presence of the environmental trigger, wherein the environmental trigger is pH or a metal ion, the method comprising:

(a) contacting the library with the target molecule to form binding complexes with protein affinity reagents, wherein the target binding interface comprises 30 to 35 amino acids;

(b) separating the binding complexes from unbound library protein affinity reagents; and

(c) eluting a population of the binding complexes that are sensitive to the environmental trigger.

2. The method of claim 1 , wherein the method further comprises step (d) selecting the population of eluted reagents on the basis of the ability to bind the target molecule in the presence of a specific environmental trigger and remain unbound in the absence of the environmental trigger.

3. The method of claim 1 , wherein the library is produced in a prokaryotic, eukaryotic or in vitro expression system, or by chemical synthesis.

4. The method of claim 1 , wherein the library is produced in a prokaryotic system.

5. The method of claim 1 , wherein the library is produced in a eukaryotic system.

6. The method of claim 1 , wherein the ionizable amino acid residues are selected from the group consisting of histidine, arginine, lysine, aspartic acid, and glutamic acid residues.

7. The method of claim 6 , wherein the ionizable amino acid residues are histidine residues.

8. The method of claim 6 , wherein the ionizable amino acid residues are arginine residues.

9. The method of claim 6 , wherein the ionizable amino acid residues are aspartic acid residues.

10. The method of claim 2 , wherein the method further comprises step (e) isolating the selected population of eluted reagents via purification.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 5, 2021
From: BOARD OF TRUSTEES OF NORTHERN ILLINOIS UNIVERSITY
To: NORTHERN ILLINOIS RESEARCH FOUNDATION
Reel/Frame 054814/0120 →
Continuity (4)
Division 13848547 · Mar 21, 2013
Continuation In Part PCTUS2011054021 · Sep 29, 2011
Provisional Application 61388215 · Sep 30, 2010
Related Publication 20180230457A1 · Aug 16, 2018