A comparative study of synthetic winged peptides for absolute protein quantification
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F21%3A00119158" target="_blank" >RIV/00216224:14310/21:00119158 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41598-021-90087-9" target="_blank" >https://www.nature.com/articles/s41598-021-90087-9</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-021-90087-9" target="_blank" >10.1038/s41598-021-90087-9</a>
Alternative languages
Result language
angličtina
Original language name
A comparative study of synthetic winged peptides for absolute protein quantification
Original language description
A proper internal standard choice is critical for accurate, precise, and reproducible mass spectrometry-based proteomics assays. Synthetic isotopically labeled (SIL) proteins are currently considered the gold standard. However, they are costly and challenging to obtain. An alternative approach uses SIL peptides or SIL "winged" peptides extended at C- or/and N-terminus with an amino acid sequence or a tag cleaved during enzymatic proteolysis. However, a consensus on the design of a winged peptide for absolute quantification is missing. In this study, we used human serum albumin as a model system to compare the quantitative performance of reference SIL protein with four different designs of SIL winged peptides: (i) commercially available SIL peptides with a proprietary trypsin cleavable tag at C-terminus, (ii) SIL peptides extended with five amino acid residues at C-terminus, (iii) SIL peptides extended with three and (iv) with five amino acid residues at both C- and N-termini. Our results demonstrate properties of various SIL extended peptides designs, e.g., water solubility and efficiency of trypsin enzymatic cleavage with primary influence on quantitative performance. SIL winged peptides extended with three amino acids at both C- and N-termini demonstrated optimal quantitative performance, equivalent to the SIL protein.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10700 - Other natural sciences
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Scientific Reports
ISSN
2045-2322
e-ISSN
—
Volume of the periodical
11
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
10
Pages from-to
1-10
UT code for WoS article
000659135700009
EID of the result in the Scopus database
2-s2.0-85106935328