Protein surface remodeling

A protein, green fluorescent protein technology, applied in the field of protein surface reconstruction, can solve problems such as aggregation troubles

Inactive Publication Date: 2009-07-22
PRESIDENT & FELLOWS OF HARVARD COLLEGE
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  • Abstract
  • Description
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Problems solved by technology

Aggregation is a particularly troublesome problem

Method used

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  • Protein surface remodeling
  • Protein surface remodeling
  • Protein surface remodeling

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example 1

[0269] Example 1 - Supercharging Proteins Can Confer Great Resilience (Resilience)

[0270] Protein aggregation is a well-known cause of human disease (Cohen, F.E.; Kelly, J.W., Nature 2003, 426, (6968), 905-9; Chiti, F. ); Dobson (Dobson, C.M), Annu Rev Biochem 2006, 75, 333-66; each incorporated herein by reference), are also major challenges facing the use of proteins as therapeutic or diagnostic agents. Problems (Frokjaer, S.; Otzen, D.E., Nature Reviews: Nat Rev Drug Discov 2005, 4, (4), 298-306; Fowler, S.B.); Poon, S.; Muff, R.; Chiti, F.; Dobson, C.M.; Zurdo, J., National Academy of Sciences Proc. (Proc Natl Acad Sci USA) 2005, 102, (29), 10105-10; each incorporated herein by reference). Knowledge of the problem of protein aggregation has been gained from the study of natural proteins. We already know that proteins are least soluble when they carry an isoelectric point of zero net charge (Loeb, J., J Gen Physiol 1921, 4, 547-555, incorporated herein by reference mi...

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Abstract

Aggregation is a major cause of the misbehavior of proteins. A system for modifying a protein to create a more stable variant is provided. The method involves identifying non-conserved hydrophobic amino acid residues on the surface of a protein, suitable for mutating to more hydrophilic residues (e.g., charged amino acids). Any number of residues on the surface may be changed to create a variant that is more soluble, resistant to aggregation, has a greater ability to re-fold, and/or is more stable under a variety of conditions. The invention also provides GFP, streptavidin, and GST variants with an increased theoretical net charge created by the inventive technology. Kits are also provided for carrying out such modifications on any protein of interest.

Description

[0001] Related applications [0002] This application claims priority under 35 U.S.C. §119(e) to U.S. Provisional Patent Application USSN 60 / 810,364, filed June 2, 2006, the entire contents of which are incorporated herein by reference. [0003] governmental support [0004] Research described herein was supported in part by a National Institutes of Health grant (GM065400). The United States Government may have certain rights in this invention. technical field [0005] none Background technique [0006] Proteins are the main building blocks of cells. Proteins catalyze chemical reactions, transduce signals in biological systems, provide structural elements in cells and extracellular matrices, act as messengers, etc. One of the main causes of poor protein performance is aggregation. This is not just a problem in the laboratory, but in many diseases, such as Alzheimer's disease. Aggregation is a particularly troublesome problem when arriving at computationally designed...

Claims

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Application Information

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IPC IPC(8): G01N33/50
Inventor 大卫·R·刘凯文·约翰·菲利普斯迈克尔·S·劳伦斯
Owner PRESIDENT & FELLOWS OF HARVARD COLLEGE
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