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From the same journal

New experimental evidence for in-chain amino acid racemization of serine in a model peptide

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New experimental evidence for in-chain amino acid racemization of serine in a model peptide. / Demarchi, Beatrice; Collins, Matthew; Bergström, Ed; Dowle, Adam; Penkman, Kirsty; Thomas-Oates, Jane; Wilson, Julie.

In: Analytical Chemistry, Vol. 85, No. 12, 18.06.2013, p. 5835-5842.

Research output: Contribution to journal › Article › peer-review

Harvard

Demarchi, B, Collins, M, Bergström, E, Dowle, A, Penkman, K, Thomas-Oates, J & Wilson, J 2013, 'New experimental evidence for in-chain amino acid racemization of serine in a model peptide', Analytical Chemistry, vol. 85, no. 12, pp. 5835-5842. https://doi.org/10.1021/ac4005869

APA

Demarchi, B., Collins, M., Bergström, E., Dowle, A., Penkman, K., Thomas-Oates, J., & Wilson, J. (2013). New experimental evidence for in-chain amino acid racemization of serine in a model peptide. Analytical Chemistry, 85(12), 5835-5842. https://doi.org/10.1021/ac4005869

Vancouver

Demarchi B, Collins M, Bergström E, Dowle A, Penkman K, Thomas-Oates J et al. New experimental evidence for in-chain amino acid racemization of serine in a model peptide. Analytical Chemistry. 2013 Jun 18;85(12):5835-5842. https://doi.org/10.1021/ac4005869

Author

Demarchi, Beatrice ; Collins, Matthew ; Bergström, Ed ; Dowle, Adam ; Penkman, Kirsty ; Thomas-Oates, Jane ; Wilson, Julie. / New experimental evidence for in-chain amino acid racemization of serine in a model peptide. In: Analytical Chemistry. 2013 ; Vol. 85, No. 12. pp. 5835-5842.

Bibtex - Download

@article{06292791c01140e2b2b012e8d4f0cb3e,
title = "New experimental evidence for in-chain amino acid racemization of serine in a model peptide",
abstract = "The facile racemization of protein-bound amino acids plays an important role in the aging and pathologies of living tissues, and it can be exploited for protein geochronological studies in subfossil biominerals. However, the in-chain degradation pathways of amino acids are complex and difficult to elucidate. Serine has proven to be particularly elusive, and its ability to racemize as a peptide-bound residue (like asparagine and aspartic acid) has not been demonstrated. This study investigates the patterns of degradation of a model peptide (WNSVWAW) at elevated temperatures, quantifying the extent of racemization and peptide bond hydrolysis using reverse-phase high-performance liquid chromatography (RP-HPLC) and tracking the presence of degradation products by MALDI-MS. We provide direct evidence that, under these experimental conditions, both serine and asparagine are able to undergo racemization as internally bound residues, which shows their potential for initiating protein breakdown and provides an explanation for the presence of d-enantiomers in living mammalian tissues. {\textcopyright} 2013 American Chemical Society.",
author = "Beatrice Demarchi and Matthew Collins and Ed Bergstr{\"o}m and Adam Dowle and Kirsty Penkman and Jane Thomas-Oates and Julie Wilson",
year = "2013",
month = jun,
day = "18",
doi = "10.1021/ac4005869",
language = "English",
volume = "85",
pages = "5835--5842",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "12",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - New experimental evidence for in-chain amino acid racemization of serine in a model peptide

AU - Demarchi, Beatrice

AU - Collins, Matthew

AU - Bergström, Ed

AU - Dowle, Adam

AU - Penkman, Kirsty

AU - Thomas-Oates, Jane

AU - Wilson, Julie

PY - 2013/6/18

Y1 - 2013/6/18

N2 - The facile racemization of protein-bound amino acids plays an important role in the aging and pathologies of living tissues, and it can be exploited for protein geochronological studies in subfossil biominerals. However, the in-chain degradation pathways of amino acids are complex and difficult to elucidate. Serine has proven to be particularly elusive, and its ability to racemize as a peptide-bound residue (like asparagine and aspartic acid) has not been demonstrated. This study investigates the patterns of degradation of a model peptide (WNSVWAW) at elevated temperatures, quantifying the extent of racemization and peptide bond hydrolysis using reverse-phase high-performance liquid chromatography (RP-HPLC) and tracking the presence of degradation products by MALDI-MS. We provide direct evidence that, under these experimental conditions, both serine and asparagine are able to undergo racemization as internally bound residues, which shows their potential for initiating protein breakdown and provides an explanation for the presence of d-enantiomers in living mammalian tissues. © 2013 American Chemical Society.

AB - The facile racemization of protein-bound amino acids plays an important role in the aging and pathologies of living tissues, and it can be exploited for protein geochronological studies in subfossil biominerals. However, the in-chain degradation pathways of amino acids are complex and difficult to elucidate. Serine has proven to be particularly elusive, and its ability to racemize as a peptide-bound residue (like asparagine and aspartic acid) has not been demonstrated. This study investigates the patterns of degradation of a model peptide (WNSVWAW) at elevated temperatures, quantifying the extent of racemization and peptide bond hydrolysis using reverse-phase high-performance liquid chromatography (RP-HPLC) and tracking the presence of degradation products by MALDI-MS. We provide direct evidence that, under these experimental conditions, both serine and asparagine are able to undergo racemization as internally bound residues, which shows their potential for initiating protein breakdown and provides an explanation for the presence of d-enantiomers in living mammalian tissues. © 2013 American Chemical Society.

UR - http://www.scopus.com/inward/record.url?scp=84879225189&partnerID=8YFLogxK

U2 - 10.1021/ac4005869

DO - 10.1021/ac4005869

M3 - Article

C2 - 23705982

VL - 85

SP - 5835

EP - 5842

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 12

ER -

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