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Modeling the structure of crystalline alamethicin and its NMR chemical shift tensors

SYSNO ASEP	0546945
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Modeling the structure of crystalline alamethicin and its NMR chemical shift tensors
Author(s)	Czernek, Jiří (UMCH-V)_RID Brus, Jiří (UMCH-V)_{RID, ORCID}
Article number	1265
Source Title	Antibiotics (Basel). - : MDPI - ISSN 2079-6382 Roč. 10, č. 10 (2021)
Number of pages	12 s.
Language	eng - English
Country	CH - Switzerland
Keywords	antimicrobial peptides ; alamethicin ; solid-state NMR
Subject RIV	CF - Physical ; Theoretical Chemistry
OECD category	Physical chemistry
R&D Projects	LTAUSA18011 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
Research Infrastructure	e-INFRA CZ - 90140 - CESNET, zájmové sdružení právnických osob ELIXIR-CZ - 90047 - Ústav organické chemie a biochemie AV ČR, v. v. i.
Method of publishing	Open access
Institutional support	UMCH-V - RVO:61389013
UT WOS	000715441600001
EID SCOPUS	85118200430
DOI	10.3390/antibiotics10101265
Annotation	Alamethicin (ALM) is an antimicrobial peptide that is frequently employed in studies of the mechanism of action of pore-forming molecules. Advanced techniques of solid-state NMR spectroscopy (SSNMR) are important in these studies, as they are capable of describing the alignment of helical peptides, such as ALM, in lipid bilayers. Here, it is demonstrated how an analysis of the SSNMR measurements can benefit from fully periodic calculations, which employ the plane-wave density-functional theory (PW DFT) of the solid-phase geometry and related spectral parameters of ALM. The PW DFT calculations are used to obtain the structure of desolvated crystalline ALM and predict the NMR chemical shift tensors (CSTs) of its nuclei. A variation in the CSTs of the amidic nitrogens and carbonyl carbons along the ALM backbone is evaluated and included in simulations of the orientation-dependent anisotropic 15N and 13C chemical shift components. In this way, the influence of the site-specific structural effects on the experimentally determined orientation of ALM is shown in models of cell membranes.
Workplace	Institute of Macromolecular Chemistry
Contact	Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358
Year of Publishing	2022
Electronic address	https://www.mdpi.com/2079-6382/10/10/1265

Number of the records: 1