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Protein Science (2001), 10:735-740.
Copyright © 2001 The Protein Society

Reactivity of peptidyl-tyrosine to hydroxylation and cross-linking

Luis A. Burzio1 and J. Herbert Waite2

1 Surgical Sealants, Inc., Woburn, Massachusetts 01801, USA
2 Marine Sciences Institute, MCDB Department, University of California, Santa Barbara, California 93106, USA

Reprint requests to: Luis A. Burzio, Surgical Sealants, Inc., 150 New Boston Street, Woburn, MA 01801, USA; e-mail: burzio{at}surgicalsealants.com; fax: (781) 937-8180.

Tyrosine residues of neuroendocrine peptides are frequently the targets of oxidation reactions, one of which involves hydroxylation to peptidyl-3, 4-dihydroxy-phenyl-L-alanine (DOPA). The reactivity in vitro of peptidyl-DOPA in two neuroendocrine peptides, a neurotensin fragment (pELYENK) and proctolin (RYLPT), was investigated using ultraviolet-visible scanning spectrophotometry and matrix-assisted laser desorption ionization mass spectrometry following oxidation by tyrosinase and periodate. The peptides form covalently coupled dimers and trimers, and their masses are consistent with the presence of diDOPA cross-links. Lysine does not appear to participate in multimer formation because it is efficiently recovered in fragmentation ladders using subtilisin. While multimer formation in the neurotensin-derived peptide can be blocked effectively by adding N-acetyl-DOPA-ethylester to the reaction medium, the DOPA ethylester couples itself four to five times to each peptide.

Keywords: Neuroendocrine; tyrosine; DOPA peptides; cross-linking; tyrosinase


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Copyright © 2001 by The Protein Society.