Facile Method of Protein PEGylation by a Mono-Ion Complex | Zendy

Shoichiro Asayama | Zendy; Kagashima | Zendy; Hiroyoshi Kawakami | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Facile Method of Protein PEGylation by a Mono-Ion Complex

Author(s) -

Shoichiro Asayama,

Kagashima,

Hiroyoshi Kawakami

Publication year - 2017

Publication title -

acs omega

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.779

H-Index - 40

ISSN - 2470-1343

DOI - 10.1021/acsomega.7b00462

Subject(s) - pegylation , catalase , chemistry , size exclusion chromatography , circular dichroism , peg ratio , trypsin , chromatography , ethylene glycol , conjugate , polyacrylamide gel electrophoresis , covalent bond , enzyme , biochemistry , polyethylene glycol , organic chemistry , mathematical analysis , mathematics , finance , economics

Diethylaminoethyl end-modified poly(ethylene glycol) (DEAE-PEG) has been synthesized for the noncovalent PEGylation of proteins. The resulting DEAE-PEG and catalase formed an ion complex, that is, a protein mono-ion complex (MIC). The formation of the protein MIC was confirmed by native poly(acrylamide) gel electrophoresis and gel-filtration chromatography. The resulting catalase MIC preserved the catalase activity, confirmed by monitoring the O 2 concentration with a Clark-type oxygen electrode, in spite of MIC formation. The catalase activity of the protein MIC was protected in the presence of a protease, trypsin, or 10% fetal bovine serum. Furthermore, less change in the circular dichroism measurements of the catalase MIC was observed as compared to those of a catalase-PEG conjugate (covalent PEGylation), suggesting less influence of the protein conformation. Consequently, the formation of the MIC is considered to be a facile method of protein PEGylation.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research