TY  - CONF
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Jovanović, Vesna
AU  - Smiljanić, Katarina
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2052
AB  - Porcine-derived trypsin generated proteomic data of the major peanut allergen Ara h 1
from the peanut was reassessed to search for possible facilitating/hindrance effects on
trypsin digestion efficacy caused by post-translational and chemical modifications (PTMs)
positioned on arginine or lysine (K/R) residues. If the potential effects caused by PTMs are
observed with porcine trypsin, they can be just augmented and more pronounced within
human intestinal digestion. The reasoning is in inferior performance of human trypsin
compared to porcine-derived used in proteomic digestion protocols, also in the lower
trypsin-to-sample ratio and much shorter digestion times, even though gastric digestion
precedes and trypsin is not the sole digestive enzyme.
A novel method was developed to decipher cleavage or miscleavage outcomes at scissile
bonds in each, modified and unmodified sequence counterparts, using PEAKS Studio-X+
(Bioinformatics Solutions Inc., Ontario, Canada) in the reassessment of high-resolution
tandem mass spectrometry data, from 18-hour long trypsin digestion proteomic protocols.
In general, eight site-specific and modified K/R residues with methylation, dihydroxy
and formylation showed significantly higher content of miscleaved bonds (at least >10%)
compared to their unmodified counterpart peptides. Specifically, dihydroxylation and
formylation hindered trypsin efficacy, while methylation on several K/R showed opposite
effects.
It is essential to elucidate the specific impacts of modifications on trypsin digestion
performance and if there are additional effects generated by food processing, which could
influence digestion outcomes and allergenicity of food proteins/peptides.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes
EP  - 107
SP  - 107
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2052
ER  - 

@conference{
author = "Prodić, Ivana and Đukić, Teodora and Jovanović, Vesna and Smiljanić, Katarina",
year = "2023",
abstract = "Porcine-derived trypsin generated proteomic data of the major peanut allergen Ara h 1
from the peanut was reassessed to search for possible facilitating/hindrance effects on
trypsin digestion efficacy caused by post-translational and chemical modifications (PTMs)
positioned on arginine or lysine (K/R) residues. If the potential effects caused by PTMs are
observed with porcine trypsin, they can be just augmented and more pronounced within
human intestinal digestion. The reasoning is in inferior performance of human trypsin
compared to porcine-derived used in proteomic digestion protocols, also in the lower
trypsin-to-sample ratio and much shorter digestion times, even though gastric digestion
precedes and trypsin is not the sole digestive enzyme.
A novel method was developed to decipher cleavage or miscleavage outcomes at scissile
bonds in each, modified and unmodified sequence counterparts, using PEAKS Studio-X+
(Bioinformatics Solutions Inc., Ontario, Canada) in the reassessment of high-resolution
tandem mass spectrometry data, from 18-hour long trypsin digestion proteomic protocols.
In general, eight site-specific and modified K/R residues with methylation, dihydroxy
and formylation showed significantly higher content of miscleaved bonds (at least >10%)
compared to their unmodified counterpart peptides. Specifically, dihydroxylation and
formylation hindered trypsin efficacy, while methylation on several K/R showed opposite
effects.
It is essential to elucidate the specific impacts of modifications on trypsin digestion
performance and if there are additional effects generated by food processing, which could
influence digestion outcomes and allergenicity of food proteins/peptides.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes",
pages = "107-107",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2052"
}

Prodić, I., Đukić, T., Jovanović, V.,& Smiljanić, K.. (2023). The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes. in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 107-107.
https://hdl.handle.net/21.15107/rcub_imagine_2052

Prodić I, Đukić T, Jovanović V, Smiljanić K. The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes. in 4th Belgrade Bioinformatics Conference. 2023;4:107-107.
https://hdl.handle.net/21.15107/rcub_imagine_2052 .

Prodić, Ivana, Đukić, Teodora, Jovanović, Vesna, Smiljanić, Katarina, "The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes" in 4th Belgrade Bioinformatics Conference, 4 (2023):107-107,
https://hdl.handle.net/21.15107/rcub_imagine_2052 .