Spontaneous Cleavage of Proteins at Serine Residues |
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Authors: | Brian Lyons Joanne Jamie Roger JW Truscott |
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Institution: | (1) Save Sight Institute, University of Sydney, Sydney Eye Hospital, 8 Macquarie St., Sydney, NSW, 2001, Australia;(2) Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia |
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Abstract: | Long-lived proteins are found at several sites in the body and they undergo numerous changes as a result of prolonged exposure
to physiological conditions. Truncation is a common modification and many cleavages appear to be non-enzymatic, however little
is known about the processes involved. In this study we demonstrate, using synthetic peptides that incorporate the sequence
of a protein that is known to cleave in older lenses, that truncation on the N-terminal side of serine residues can occur at neutral pH. A mechanism that incorporates an N,O-acyl shift, which is analogous to intein cleavage, is proposed. Such cleavages may explain the origin of abundant peptides
derived from crystallins in aged human lenses. |
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