Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity

The in silico modelling of peptides complementary to lactoferrin was carried out using the Protein 3D software package and replication of the natural bonding site between pneumococcal surface protein (PSP) and lactoferrin (LF). The modeling was based on analysis of the conjugated ion–hydrogen bond s...

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Main Authors: Tatiana Zimina, Nikita Sitkov, Vladimir Karasev, Yury Skorik, Alexey Kolobov, Alexander Kolobov, Nikolay Bunenkov, Viktor Luchinin
Format: Article
Language:English
Published: MDPI AG 2023-02-01
Series:Chemosensors
Subjects:
Online Access:https://www.mdpi.com/2227-9040/11/3/162
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author Tatiana Zimina
Nikita Sitkov
Vladimir Karasev
Yury Skorik
Alexey Kolobov
Alexander Kolobov
Nikolay Bunenkov
Viktor Luchinin
author_facet Tatiana Zimina
Nikita Sitkov
Vladimir Karasev
Yury Skorik
Alexey Kolobov
Alexander Kolobov
Nikolay Bunenkov
Viktor Luchinin
author_sort Tatiana Zimina
collection DOAJ
description The in silico modelling of peptides complementary to lactoferrin was carried out using the Protein 3D software package and replication of the natural bonding site between pneumococcal surface protein (PSP) and lactoferrin (LF). The modeling was based on analysis of the conjugated ion–hydrogen bond systems between these proteins (CIHBS). The oligopeptide EEVAPQAQAKIAELENQVHRLE was proposed via computer modelling and synthesized using the solid phase synthesis technique, purified, and analyzed with MS and HPLC methods to confirm >95% purity. The peptide was then studied by capillary electrophoresis (CE). The CE experiments demonstrated the split of peptide zone in the presence of LF, due to complex formation and subsequent mobility change of the system peptide-protein. The reference experiments with homomyeloperoxidase and myoglobin did not show binding with LETI-11.
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spelling doaj.art-75205972fda44ceab4d345491a9df4c72023-11-17T10:16:07ZengMDPI AGChemosensors2227-90402023-02-0111316210.3390/chemosensors11030162Design of Peptide Ligand for Lactoferrin and Study of Its Binding SpecificityTatiana Zimina0Nikita Sitkov1Vladimir Karasev2Yury Skorik3Alexey Kolobov4Alexander Kolobov5Nikolay Bunenkov6Viktor Luchinin7Department of Micro and Nanoelectronics, Saint Petersburg Electrotechnical University “LETI”, 197022 Saint Petersburg, RussiaDepartment of Micro and Nanoelectronics, Saint Petersburg Electrotechnical University “LETI”, 197022 Saint Petersburg, RussiaDepartment of Micro and Nanoelectronics, Saint Petersburg Electrotechnical University “LETI”, 197022 Saint Petersburg, RussiaAlmazov National Medical Research Centre, 197341 Saint Petersburg, RussiaCentre for Digital Telecommunication Technologies, Saint Petersburg Electrotechnical University “LETI”, 197022 Saint Petersburg, RussiaLaboratory of Peptide Chemistry, Institute of Human Hygiene, Occupational Pathology and Ecology, 188663 Saint Petersburg, RussiaDepartment of Bone Marrow Transplantation, Raisa Gorbacheva Research Institute of Children Oncology, Hematology and Transplantation of Pavlov First Saint Petersburg State Medical University, 197022 Saint Petersburg, RussiaDepartment of Micro and Nanoelectronics, Saint Petersburg Electrotechnical University “LETI”, 197022 Saint Petersburg, RussiaThe in silico modelling of peptides complementary to lactoferrin was carried out using the Protein 3D software package and replication of the natural bonding site between pneumococcal surface protein (PSP) and lactoferrin (LF). The modeling was based on analysis of the conjugated ion–hydrogen bond systems between these proteins (CIHBS). The oligopeptide EEVAPQAQAKIAELENQVHRLE was proposed via computer modelling and synthesized using the solid phase synthesis technique, purified, and analyzed with MS and HPLC methods to confirm >95% purity. The peptide was then studied by capillary electrophoresis (CE). The CE experiments demonstrated the split of peptide zone in the presence of LF, due to complex formation and subsequent mobility change of the system peptide-protein. The reference experiments with homomyeloperoxidase and myoglobin did not show binding with LETI-11.https://www.mdpi.com/2227-9040/11/3/162peptide aptamersbiosensorslactoferrinelectrophoresisligands
spellingShingle Tatiana Zimina
Nikita Sitkov
Vladimir Karasev
Yury Skorik
Alexey Kolobov
Alexander Kolobov
Nikolay Bunenkov
Viktor Luchinin
Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
Chemosensors
peptide aptamers
biosensors
lactoferrin
electrophoresis
ligands
title Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
title_full Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
title_fullStr Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
title_full_unstemmed Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
title_short Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
title_sort design of peptide ligand for lactoferrin and study of its binding specificity
topic peptide aptamers
biosensors
lactoferrin
electrophoresis
ligands
url https://www.mdpi.com/2227-9040/11/3/162
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