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Effect of Peptide Primary Sequence on Biuret Complex Formation and Properties
Author(s) -
Chen JianGe,
Logman Michael,
Weber Stephen G.
Publication year - 1999
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/(sici)1521-4109(199905)11:5<331::aid-elan331>3.0.co;2-#
Subject(s) - biuret test , sequence (biology) , primary (astronomy) , peptide , chemistry , biochemistry , physics , urea , astronomy
Visible spectroscopy and the rotating ring‐disk electrode were used to study Cu(II)‐peptide complexation of 21 peptides including N‐acylated and N‐pyroglutamyl peptides. All of the investigated peptides formed a complex with copper ion, and those complexes were electroactive. Peptides containing proline near the amine terminus, and N‐acylated peptides, had lower rate constants for the formation of the electroactive complexes. Reaction rates were not significantly decreased in peptides with a pyroglutamyl amine terminus. These complexes demonstrated very low oxidation potentials and some unusual spectroscopic properties.