Biomaterial Database

Improving Properties of Recombinant SsoPox by Site-Specific Pegylation. 2015

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

SsoPox, a ~35 kDa enzyme from Sulfolobus solfataricus, can hydrolyze and inactivate a variety of organophosphate (OP)-compounds. The enzyme is a potential candidate for the development of prophylactic and therapeutic agent against OP-poisoning in humans. However, the therapeutic use of recombinant SsoPox suffers from certain limitations associated with the use of recombinant protein pharmaceuticals. Some of these limitations could be overcome by conjugating SsoPox enzyme with polyethylene glycol (PEG). In this study, we report generation and in vitro characterization of N-terminal mono-PEGylated rSsoPox(2p) (a variant of rSsoPox(wt) having enhanced OP-hydrolyzing activity). The enzyme was PEGylated with mPEG-propionaldehyde and the PEGylated protein was isolated using ion-exchange chromatography. Compared with the unmodified enzyme, mono-PEGylation of rSsoPox results in improvement in the thermostability and protease resistance of the enzyme. PEGylated rSsoPox(2p) can be developed as a candidate for the prevention / treatment of OP-poisoning.

UI	MeSH Term	Description	Entries
D011092	Polyethylene Glycols	Polymers of ETHYLENE OXIDE and water, and their ethers. They vary in consistency from liquid to solid depending on the molecular weight indicated by a number following the name. They are used as SURFACTANTS, dispersing agents, solvents, ointment and suppository bases, vehicles, and tablet excipients. Some specific groups are NONOXYNOLS, OCTOXYNOLS, and POLOXAMERS.	Macrogols,Polyoxyethylenes,Carbowax,Macrogol,Polyethylene Glycol,Polyethylene Oxide,Polyethyleneoxide,Polyglycol,Glycol, Polyethylene,Glycols, Polyethylene,Oxide, Polyethylene,Oxides, Polyethylene,Polyethylene Oxides,Polyethyleneoxides,Polyglycols,Polyoxyethylene
D011994	Recombinant Proteins	Proteins prepared by recombinant DNA technology.	Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004795	Enzyme Stability	The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.	Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D000581	Amidohydrolases	Any member of the class of enzymes that catalyze the cleavage of amide bonds and result in the addition of water to the resulting molecules.	Amidases,Amidohydrolase
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D044345	Phosphoric Triester Hydrolases	A class of enzymes that catalyze the hydrolysis of one of the three ester bonds in a phosphotriester-containing compound.	Phosphotriesterase,Hydrolases, Phosphoric Triester,Triester Hydrolases, Phosphoric
D048229	Sulfolobus solfataricus	A species of thermoacidophilic ARCHAEA in the family Sulfolobaceae, found in volcanic areas where the temperature is about 80 degrees C and SULFUR is present.

Related Publications

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

[Site-specific PEGylation of recombinant lysostaphin].

January 2016, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

Site-specific PEGylation of recombinant tissue-type plasminogen activator.

November 2023, European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V,

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

Recombinant protein hydrazides: application to site-specific protein PEGylation.

June 2011, Bioconjugate chemistry,

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

Site-Specific PEGylation of Therapeutic Proteins.

October 2015, International journal of molecular sciences,

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

Site-specific pegylation of G-CSF by reversible denaturation.

January 2007, Bioconjugate chemistry,

Harsh Parikh, and Priyanka Bajaj, and Rajan K Tripathy, and Abhay H Pande

Tailoring structure-function and pharmacokinetic properties of single-chain Fv proteins by site-specific PEGylation.

October 2003, Protein engineering,