Modification of protein with BGL06, a novel branched oligoglycerol derivative

Biochimica Et Biophysica Acta
Hiroyuki YamaguchiMotoo Yamasaki

Abstract

A branched oligoglycerol derivative, BGL06, with a cascade-like structure of glycerol units was used as a novel reagent for protein modification. Modification reaction with a recombinant human granulocyte-colony stimulating factor derivative, ND28, was carried out successfully in aqueous conditions to obtain a coupled form, BGL06-ND28. Characterization of the modified ND28 suggests that two types of products were obtained by controlling the reaction; one was H(BGL06)-ND28, a highly modified version coupled with 4.34 molecules of BGL06 units on average, and the other was L(BGL06)-ND28, a moderately modified version coupled with 2.58 molecules of BGL06 units on average, respectively. The properties of these products were compared to the known polyethylene glycol (PEG)-modified ND28. In the cell proliferation assays, unlike PEGylation, modification with BGL06 did not produce a significant loss of biological activity even when the modification extent was elevated. Under such conditions, 76.0% of the activity was in fact maintained for H(BGL06)-ND28, while PEGylated ND28 retained only 24.6% of biological activity in vitro even though the extent of modification was smaller. In addition, H(BGL06)-ND28 showed comparable thermostability...Continue Reading

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Citations

Mar 20, 2010·International Journal of Pharmaceutics·Atsushi IshiharaMotoo Yamasaki
Jan 20, 2009·Biochimica Et Biophysica Acta·Margherita Gonnelli, Giovanni B Strambini
Nov 8, 2011·Journal of Biomaterials Science. Polymer Edition·Atsushi IshiharaMotoo Yamasaki
May 26, 2009·Journal of the American Chemical Society·Frederik WurmHolger Frey

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