Publication

Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry

Zhang, T., Niu, X., Yuan, T., Tessari, M., de Vries, M. P., Permentier, H. P. & Bischoff, R., 21-Jun-2016, In : Analytical Chemistry. 88, 12, p. 6465-6471 7 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Zhang, T., Niu, X., Yuan, T., Tessari, M., de Vries, M. P., Permentier, H. P., & Bischoff, R. (2016). Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry. Analytical Chemistry, 88(12), 6465-6471. https://doi.org/10.1021/acs.analchem.6b01154

Author

Zhang, Tao ; Niu, Xiaoyu ; Yuan, Tao ; Tessari, Marco ; de Vries, Marcel P. ; Permentier, Hjalmar P. ; Bischoff, Rainer. / Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry. In: Analytical Chemistry. 2016 ; Vol. 88, No. 12. pp. 6465-6471.

Harvard

Zhang, T, Niu, X, Yuan, T, Tessari, M, de Vries, MP, Permentier, HP & Bischoff, R 2016, 'Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry', Analytical Chemistry, vol. 88, no. 12, pp. 6465-6471. https://doi.org/10.1021/acs.analchem.6b01154

Standard

Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry. / Zhang, Tao; Niu, Xiaoyu; Yuan, Tao; Tessari, Marco; de Vries, Marcel P.; Permentier, Hjalmar P.; Bischoff, Rainer.

In: Analytical Chemistry, Vol. 88, No. 12, 21.06.2016, p. 6465-6471.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Zhang T, Niu X, Yuan T, Tessari M, de Vries MP, Permentier HP et al. Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry. Analytical Chemistry. 2016 Jun 21;88(12):6465-6471. https://doi.org/10.1021/acs.analchem.6b01154


BibTeX

@article{dbb8d212f7bd4abcb650704055b2af66,
title = "Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry",
abstract = "Specific digestion of proteins is an essential step for mass spectrometry-based proteomics, and the chemical labeling of the resulting peptides is often used for peptide enrichment or the introduction of desirable tags. Cleavage of the peptide bond following electrochemical oxidation of Tyr or Trp results in a spirolactone moiety at the newly formed C-terminus offering a handle for chemical labeling. In this work, we developed a highly efficient and selective chemical labeling approach based on spirolactone chemistry. Electrochemically generated peptide-spirolactones readily undergo an intramolecular rearrangement yielding isomeric diketopiperazines precluding further chemical labeling. A strategy was established to prevent intramolecular arrangement by acetylating the N-terminal amino group prior to electrochemical oxidation and cleavage allowing the complete and selective chemical labeling of the tripeptide LWL and the decapeptide ACTH 1-10 with amine-containing reagents. As examples, we show the successful introduction of a fluorescent label and biotin for detection or affinity enrichment. Electrochemical digestion of peptides and proteins followed by efficient chemical labeling constitutes a new, powerful tool in protein chemistry and protein analysis.",
keywords = "MASS-SPECTROMETRIC DETECTION, INTRAMOLECULAR AMINOLYSIS, PROTEIN DIGESTION, ORGANIC-SOLVENTS, PROTEOMICS, CLEAVAGE, OXIDATION, TRYPSIN, IDENTIFICATION, STRATEGIES",
author = "Tao Zhang and Xiaoyu Niu and Tao Yuan and Marco Tessari and {de Vries}, {Marcel P.} and Permentier, {Hjalmar P.} and Rainer Bischoff",
year = "2016",
month = jun,
day = "21",
doi = "10.1021/acs.analchem.6b01154",
language = "English",
volume = "88",
pages = "6465--6471",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "AMER CHEMICAL SOC INC",
number = "12",

}

RIS

TY - JOUR

T1 - Efficient and Selective Chemical Labeling of Electrochemically Generated Peptides Based on Spirolactone Chemistry

AU - Zhang, Tao

AU - Niu, Xiaoyu

AU - Yuan, Tao

AU - Tessari, Marco

AU - de Vries, Marcel P.

AU - Permentier, Hjalmar P.

AU - Bischoff, Rainer

PY - 2016/6/21

Y1 - 2016/6/21

N2 - Specific digestion of proteins is an essential step for mass spectrometry-based proteomics, and the chemical labeling of the resulting peptides is often used for peptide enrichment or the introduction of desirable tags. Cleavage of the peptide bond following electrochemical oxidation of Tyr or Trp results in a spirolactone moiety at the newly formed C-terminus offering a handle for chemical labeling. In this work, we developed a highly efficient and selective chemical labeling approach based on spirolactone chemistry. Electrochemically generated peptide-spirolactones readily undergo an intramolecular rearrangement yielding isomeric diketopiperazines precluding further chemical labeling. A strategy was established to prevent intramolecular arrangement by acetylating the N-terminal amino group prior to electrochemical oxidation and cleavage allowing the complete and selective chemical labeling of the tripeptide LWL and the decapeptide ACTH 1-10 with amine-containing reagents. As examples, we show the successful introduction of a fluorescent label and biotin for detection or affinity enrichment. Electrochemical digestion of peptides and proteins followed by efficient chemical labeling constitutes a new, powerful tool in protein chemistry and protein analysis.

AB - Specific digestion of proteins is an essential step for mass spectrometry-based proteomics, and the chemical labeling of the resulting peptides is often used for peptide enrichment or the introduction of desirable tags. Cleavage of the peptide bond following electrochemical oxidation of Tyr or Trp results in a spirolactone moiety at the newly formed C-terminus offering a handle for chemical labeling. In this work, we developed a highly efficient and selective chemical labeling approach based on spirolactone chemistry. Electrochemically generated peptide-spirolactones readily undergo an intramolecular rearrangement yielding isomeric diketopiperazines precluding further chemical labeling. A strategy was established to prevent intramolecular arrangement by acetylating the N-terminal amino group prior to electrochemical oxidation and cleavage allowing the complete and selective chemical labeling of the tripeptide LWL and the decapeptide ACTH 1-10 with amine-containing reagents. As examples, we show the successful introduction of a fluorescent label and biotin for detection or affinity enrichment. Electrochemical digestion of peptides and proteins followed by efficient chemical labeling constitutes a new, powerful tool in protein chemistry and protein analysis.

KW - MASS-SPECTROMETRIC DETECTION

KW - INTRAMOLECULAR AMINOLYSIS

KW - PROTEIN DIGESTION

KW - ORGANIC-SOLVENTS

KW - PROTEOMICS

KW - CLEAVAGE

KW - OXIDATION

KW - TRYPSIN

KW - IDENTIFICATION

KW - STRATEGIES

U2 - 10.1021/acs.analchem.6b01154

DO - 10.1021/acs.analchem.6b01154

M3 - Article

C2 - 27247048

VL - 88

SP - 6465

EP - 6471

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 12

ER -

ID: 32803297