KFU. Card publication. Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles

KAZAN
FEDERAL UNIVERSITY

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SPATIAL STRUCTURE OF THE FIBRIL-FORMING SEM1(86&NDASH;107) PEPTIDE IN A COMPLEX WITH DODECYLPHOSPHOCHOLINE MICELLES

Form of presentation

Articles in Russian journals and collections

Year of publication

2022

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Authors, employees of KFU

Bikmullin Aydar Galimzanovich, author

Blokhin Dmitriy Sergeevich, author

Klochkov Vladimir Vasilevich, author

Authors, students KFU

Osetrina Darya Andreevna, author

Bibliographic description in the original language

Sanchugova D.A. Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles / Sanchugova D.A., Bikmullin A.G., Klochkov V.V., Aganov A.V., Blokhin D.S. // Russian Chemical Bulletin. – 2022. – V. 70 (12). – R. 2422 – 2426.

Annotation

SEM1(86-107) peptide is a cleavage product of semenogelin 1 (SEM1) expressed in seminal vesicles. SEM1(86-107) forms amyloid fibrils in semen increasing HIV infectivity by up to 3–5 orders of magnitude. The study of fibrillation process includes peptide spatial structure determination. This paper presents the information about the SEM1(86-107) structure obtained by the Nuclear Magnetic Resonance (NMR) spectroscopy and Circular Dichroism (CD) spectroscopy. Assignment of hydrogen chemical shifts and internuclear distances of the SEM1(86-107) with following prediction of secondary structure was carried out by the NMR spectroscopy. Also the spatial structure was calculated using the XPLOR-NIH software. The spatial structure analysis has shown the containing the regions with the random coil conformations in the SEM1(86-107) peptide. Analysis of the structure ensemble showed containing fragments with high convergence: Leu87-Lys92, Thr94-Gln97, and Gln104-Leu107. It can be assumed that these fragments are responsible for the fibrillation process via low their mobility. CD spectroscopy was applied to determine the secondary structure of SEM1(86-107). CD measurement confirmed that the prevailing secondary structure content of SEM1(86-107) peptide is a random coil.

Keywords

NMR, peptide

The name of the journal

Russian Chemical Bulletin

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

https://repository.kpfu.ru/eng/?p_id=264780&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Bikmullin Aydar Galimzanovich	ru_RU
dc.contributor.author	Blokhin Dmitriy Sergeevich	ru_RU
dc.contributor.author	Klochkov Vladimir Vasilevich	ru_RU
dc.contributor.author	Osetrina Darya Andreevna	ru_RU
dc.date.accessioned	2022-01-01T00:00:00Z	ru_RU
dc.date.available	2022-01-01T00:00:00Z	ru_RU
dc.date.issued	2022	ru_RU
dc.identifier.citation	Sanchugova D.A. Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles / Sanchugova D.A., Bikmullin A.G., Klochkov V.V., Aganov A.V., Blokhin D.S. // Russian Chemical Bulletin. – 2022. – V. 70 (12). – �. 2422 – 2426.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=264780&p_lang=2	ru_RU
dc.description.abstract	Russian Chemical Bulletin	ru_RU
dc.description.abstract	SEM1(86-107) peptide is a cleavage product of semenogelin 1 (SEM1) expressed in seminal vesicles. SEM1(86-107) forms amyloid fibrils in semen increasing HIV infectivity by up to 3–5 orders of magnitude. The study of fibrillation process includes peptide spatial structure determination. This paper presents the information about the SEM1(86-107) structure obtained by the Nuclear Magnetic Resonance (NMR) spectroscopy and Circular Dichroism (CD) spectroscopy. Assignment of hydrogen chemical shifts and internuclear distances of the SEM1(86-107) with following prediction of secondary structure was carried out by the NMR spectroscopy. Also the spatial structure was calculated using the XPLOR-NIH software. The spatial structure analysis has shown the containing the regions with the random coil conformations in the SEM1(86-107) peptide. Analysis of the structure ensemble showed containing fragments with high convergence: Leu87-Lys92, Thr94-Gln97, and Gln104-Leu107. It can be assumed that these fragments are responsible for the fibrillation process via low their mobility. CD spectroscopy was applied to determine the secondary structure of SEM1(86-107). CD measurement confirmed that the prevailing secondary structure content of SEM1(86-107) peptide is a random coil.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	NMR	ru_RU
dc.subject	peptide	ru_RU
dc.title	Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles	ru_RU
dc.type	Articles in Russian journals and collections	ru_RU