Spontaneous cleavage of proteins at serine residues | Macquarie University ResearchOnline

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Title: Spontaneous cleavage of proteins at serine residues
Related: International journal of peptide research and therapeutics, Vol. 17, No. 2, (2011), p.131-135
DOI: 10.1007/s10989-011-9250-3
Publisher: Springer
Date: 2011
Author/Creator: Lyons, B
Author/Creator: Jamie, J
Author/Creator: Truscott, R. J. W
Description: 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.
Description: 5 page(s)
Subject Keyword: Age
Subject Keyword: Human lens
Subject Keyword: Hydrolysis
Subject Keyword: Old proteins
Subject Keyword: Posttranslational modification
Resource Type: journal article
Organisation: Macquarie University. Dept. of Chemistry and Biomolecular Sciences

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