KFU. Card publication. Solution NMR studies of LPRDA peptide - an oligopeptide inhibitor of Staphylococcus aureus Sortase A

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SOLUTION NMR STUDIES OF LPRDA PEPTIDE - AN OLIGOPEPTIDE INHIBITOR OF STAPHYLOCOCCUS AUREUS SORTASE A

Form of presentation

Articles in Russian journals and collections

Year of publication

2024

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Authors, employees of KFU

Aganov Albert Vartanovich, author

Efimov Sergey Vladimirovich, author

Klochkov Vladimir Vasilevich, author

Usachev Konstantin Sergeevich, author

Bibliographic description in the original language

Kuchaev E.S., Efimov S.V., Klochkov A.V., Aganov A.V., Ivantcova P.M., Kudryavtsev K.V., Usachev K.S. Solution NMR studies of LPRDA peptide - an oligopeptide inhibitor of Staphylococcus aureus Sortase A // Applied Magnetic Resonance. – 2024. – V. 55. – P. 451-461.

Annotation

Sortases are Gram-positive bacterial extracellular transpeptidases involved in the attachment of surface proteins to the cell wall. The mechanism of action of Staphylococcus aureus Sortase A (SrtA) is based on specific recognition of the LPXTG motive at the C-terminus of the surface protein, cleavage of this site between threonine and glycine residues, subsequent transfer of the N-terminal transmembrane domain to the amino group of the pentaglycine linker and thus anchoring of proteins with this motive on the cell surface. As SrtA is involved in both early and late stages of bacterial infection because it attaches adhesins and immune evasion proteins to the cell wall, this enzyme is a good target for combating bacterial infections. The oligopeptide LPRDA was recently found to be an effective inhibitor of the enzymatic activity of SrtA through competitive binding to its active site. By NMR spectroscopy we solved the solution structure of the LPRDA peptide and showed the presence of several conformers in solution. The obtained data are the basis for further studies of the structure and function of peptidomimetics based on LPRDA oligopeptide.

Keywords

NMR, oligopeptide, Staphylococcus aureus Sortase A

The name of the journal

APPLIED MAGNETIC RESONANCE

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=306620&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Aganov Albert Vartanovich	ru_RU
dc.contributor.author	Efimov Sergey Vladimirovich	ru_RU
dc.contributor.author	Klochkov Vladimir Vasilevich	ru_RU
dc.contributor.author	Usachev Konstantin Sergeevich	ru_RU
dc.date.accessioned	2024-01-01T00:00:00Z	ru_RU
dc.date.available	2024-01-01T00:00:00Z	ru_RU
dc.date.issued	2024	ru_RU
dc.identifier.citation	Kuchaev E.S., Efimov S.V., Klochkov A.V., Aganov A.V., Ivantcova P.M., Kudryavtsev K.V., Usachev K.S. Solution NMR studies of LPRDA peptide - an oligopeptide inhibitor of Staphylococcus aureus Sortase A // Applied Magnetic Resonance. – 2024. – V. 55. – P. 451-461.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=306620&p_lang=2	ru_RU
dc.description.abstract	APPLIED MAGNETIC RESONANCE	ru_RU
dc.description.abstract	Sortases are Gram-positive bacterial extracellular transpeptidases involved in the attachment of surface proteins to the cell wall. The mechanism of action of Staphylococcus aureus Sortase A (SrtA) is based on specific recognition of the LPXTG motive at the C-terminus of the surface protein, cleavage of this site between threonine and glycine residues, subsequent transfer of the N-terminal transmembrane domain to the amino group of the pentaglycine linker and thus anchoring of proteins with this motive on the cell surface. As SrtA is involved in both early and late stages of bacterial infection because it attaches adhesins and immune evasion proteins to the cell wall, this enzyme is a good target for combating bacterial infections. The oligopeptide LPRDA was recently found to be an effective inhibitor of the enzymatic activity of SrtA through competitive binding to its active site. By NMR spectroscopy we solved the solution structure of the LPRDA peptide and showed the presence of several conformers in solution. The obtained data are the basis for further studies of the structure and function of peptidomimetics based on LPRDA oligopeptide.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	NMR	ru_RU
dc.subject	oligopeptide	ru_RU
dc.subject	Staphylococcus aureus Sortase A	ru_RU
dc.title	Solution NMR studies of LPRDA peptide - an oligopeptide inhibitor of Staphylococcus aureus Sortase A	ru_RU
dc.type	Articles in Russian journals and collections	ru_RU