Spontaneous cleavage of proteins at serine residues

Brian Lyons, Joanne Jamie, Roger J W Truscott

Research output: Contribution to journalArticleResearchpeer-review

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.

LanguageEnglish
Pages131-135
Number of pages5
JournalInternational Journal of Peptide Research and Therapeutics
Volume17
Issue number2
DOIs
Publication statusPublished - Jun 2011

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Serine
Peptides
Lenses
Inteins
Proteins
Crystallins

Cite this

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Spontaneous cleavage of proteins at serine residues. / Lyons, Brian; Jamie, Joanne; Truscott, Roger J W.

In: International Journal of Peptide Research and Therapeutics, Vol. 17, No. 2, 06.2011, p. 131-135.

Research output: Contribution to journalArticleResearchpeer-review

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