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Updated: Jul 2, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Differences in susceptibility between crystallins and non-lenticular proteins to copper and H2O2-mediated peptide
1Institute of Cancer Research, Haddow Laboratories, Belmont, Sutton, Surrey, U.K.
Abstract:
The relative susceptibilities of lenticular proteins (alpha, beta and gamma-crystallins) and a number of proteins of non-lenticular origin, to hydroxyl radical-mediated peptide bond cleavage were compared. The non-lenticular proteins (bovine serum albumin, ovalbumin, alcohol dehydrogenase, lysozyme, thyroglobulin, beta-amylase, haemoglobin and carbonic anhydrase) were readily cleaved into acid-soluble fragments following 5 hours treatment with copper ions and hydrogen peroxide. In contrast the crystallins were almost totally unaffected by similar treatment. When alpha-crystallin was pre-treated with acid or cleaved into large fragments with cyanogen bromide it became susceptible to hydroxyl radical attack, yet heating the protein did not diminish its resistance. It is suggested that the resistance of alpha-crystallin to the copper/peroxide-mediated fragmentation may be dependent on the conformation of the protein.
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