Site-specific PEGylation of Engineered Cysteine Analogues of Recombinant Human Interleukin-11
- VernacularTitle:人白细胞介素11的定点聚乙二醇修饰
- Author:
Zhi-Hua LI
;
Man-Cang HU
;
Ling-Mei YAN
;
Yu-Jiao ZHAO
;
Xu YANG
;
Zheng-Hua PENG
;
Wei-Ming XU
;
Jian-Feng LI
;
- Publication Type:Journal Article
- Keywords:
Human interleukin-11(hIL11)Polyethylene glycol Chemical modification
- From:
China Biotechnology
2006;0(06):-
- CountryChina
- Language:Chinese
-
Abstract:
Human Interleukin-11(hIL-11)has no Cys residue in its natural form.By site-directed mutagenesis,a Cys residue can be introduced to replace the 1st residue Gly and the rhIL-11 was chemically modified by using 20 kDa mPEG-maleimide conjugated to this site.The mPEG-hIL-11 conjugate was purified and showed a single band on SDS-PAGE with an apparent molecular weight.The biological activity of purified mPEG-hIL-11 was determined using a dependent cell line 7TD1.The remaining biological activity of PEGylated-rhIL-11 was 30% of native rhIL-11,suggesting chemical modification of rhIL-11 by PEG is a promising approach for improving the pharmacological efficacy.
