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

0546945 - ÚMCH 2022 RIV CH eng J - Journal Article
Czernek, Jiří - Brus, Jiří
Modeling the structure of crystalline alamethicin and its NMR chemical shift tensors.
Antibiotics (Basel). Roč. 10, č. 10 (2021), č. článku 1265. ISSN 2079-6382. E-ISSN 2079-6382
R&D Projects: GA MŠMT(CZ) LTAUSA18011
Grant - others:AV ČR(CZ) StrategieAV21/10
Program: StrategieAV
Research Infrastructure: e-INFRA CZ - 90140; ELIXIR-CZ - 90047
Institutional support: RVO:61389013
Keywords : antimicrobial peptides * alamethicin * solid-state NMR
OECD category: Physical chemistry
Impact factor: 5.222, year: 2021
Method of publishing: Open access
https://www.mdpi.com/2079-6382/10/10/1265

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.
Permanent Link: http://hdl.handle.net/11104/0323867