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Journal of Bioactive and Compatible Polymers
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An Unusual Coupling of Poly(Ethylene Glycol) to Tyrosine Residues in Epidermal Growth Factor

Laura Orsatti

Department of Pharmaceutical Sciences, University of Padova, 35131 Padova, Italy

Francesco M. Veronese

Department of Pharmaceutical Sciences, University of Padova, 35131 Padova, Italy

An unusual covalent binding of hydroxysuccinimidyl ester activated polyethylene glycol), PEG, was found in the modification of a genetic variant of mouse epidermal growth factor (EGF): PEG was bound not only to the amino groups of the polypeptide as expected, but to a tyrosine residue as well. This unexpected PEGylation is related to the tyrosine environment in the peptide which does not occur in human EGF; furthermore, it is related to PEG size since it was found to occur to a greater extent with the PEG 5,000 molecular weight, than with the more hindered PEG 10,000.

Journal of Bioactive and Compatible Polymers, Vol. 14, No. 5, 429-436 (1999)
DOI: 10.1177/088391159901400505
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