TY - JOUR
T1 - Heat-stable hazelnut profilin
T2 - Molecular dynamics simulations and immunoinformatics analysis
AU - Barazorda-Ccahuana, Haruna L.
AU - Theiss-De-Rosso, Vinicius
AU - Valencia, Diego Ernesto
AU - Gómez, Badhin
N1 - Publisher Copyright:
© 2020 by the authors.
PY - 2020/8
Y1 - 2020/8
N2 - Heat treatment can modify the allergenic potential, reducing allergenicity in specific proteins. Profilins are one of the important hazelnut allergens; these proteins are considered panallergens due to their high capacity for cross-reactivity with other allergens. In the present work, we evaluated the thermostability of hazelnut profilin, combining molecular dynamics simulation and immunoinformatic techniques. This approach helped us to have reliable results in immunogenicity studies. We modeled Cor a 2 profilin and applied annealing simulation, equilibrium, and production simulation at constant temperatures ranging from 300 to 500 K using Gromacs software. Despite the hazelnut profilins being able to withstand temperatures of up to 400 K, this does not seem to reduce its allergenicity. We have found that profilin subjected to temperatures of 450 and 500 K could generate cross-reactivity with other food allergens. In conclusion, we note a remarkable thermostability of Cor a 2 at 400 K which avoids its structural unfolding.
AB - Heat treatment can modify the allergenic potential, reducing allergenicity in specific proteins. Profilins are one of the important hazelnut allergens; these proteins are considered panallergens due to their high capacity for cross-reactivity with other allergens. In the present work, we evaluated the thermostability of hazelnut profilin, combining molecular dynamics simulation and immunoinformatic techniques. This approach helped us to have reliable results in immunogenicity studies. We modeled Cor a 2 profilin and applied annealing simulation, equilibrium, and production simulation at constant temperatures ranging from 300 to 500 K using Gromacs software. Despite the hazelnut profilins being able to withstand temperatures of up to 400 K, this does not seem to reduce its allergenicity. We have found that profilin subjected to temperatures of 450 and 500 K could generate cross-reactivity with other food allergens. In conclusion, we note a remarkable thermostability of Cor a 2 at 400 K which avoids its structural unfolding.
KW - Allergen
KW - Hazelnut
KW - Immunoinformatic
KW - Molecular dynamics simulation
KW - Profilin
UR - http://www.scopus.com/inward/record.url?scp=85089841846&partnerID=8YFLogxK
U2 - 10.3390/POLYM12081742
DO - 10.3390/POLYM12081742
M3 - Article
AN - SCOPUS:85089841846
SN - 2073-4360
VL - 12
JO - Polymers
JF - Polymers
IS - 8
M1 - 1742
ER -