作者
Cheng Yang, Diannan Lu, Zheng Liu
发表日期
2011/4/5
期刊
Biochemistry
卷号
50
期号
13
页码范围
2585-2593
出版商
American Chemical Society
简介
While the effectiveness of PEGylation in enhancing the stability and potency of protein pharmaceuticals has been validated for years, the underlying mechanism remains poorly understood, particularly at the molecular level. A molecular dynamics simulation was developed using an annealing procedure that allowed an all-atom level examination of the interaction between PEG polymers of different chain lengths and a conjugated protein represented by insulin. It was shown that PEG became entangled around the protein surface through hydrophobic interaction and concurrently formed hydrogen bonds with the surrounding water molecules. In addition to enhancing its structural stability, as indicated by the root-mean-square difference (rmsd) and secondary structure analyses, conjugation increased the size of the protein drug while decreasing the solvent accessible surface area of the protein. All these thus led to …
学术搜索中的文章
C Yang, D Lu, Z Liu - Biochemistry, 2011