Effect of TFE on the Helical Content of AK17 and HAL-1 Peptides: Theoretical Insights into the Mechanism of Helix Stabilization

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00458836" target="_blank" >RIV/61388963:_____/16:00458836 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1021/acs.jpcb.5b11228" target="_blank" >http://dx.doi.org/10.1021/acs.jpcb.5b11228</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.jpcb.5b11228" target="_blank" >10.1021/acs.jpcb.5b11228</a>

Result language

angličtina

Original language name

Effect of TFE on the Helical Content of AK17 and HAL-1 Peptides: Theoretical Insights into the Mechanism of Helix Stabilization

Original language description

Fluorinated alcohols such as 2,2,2-trifluoroethanol (TFE) are among the most frequently used, cosolvents in experiment studies of peptides. They have significant effects on secondary structure and a particularly strong promotion of alpha-helix is induced by TFE. In this study we validated recently proposed force field parameters for TFE in molecular dynamics simulations with two model peptides-alanine-rich AK-17 and antimicrobial peptide halictine-1 (HAL-1). In the case of HAL-1, we characterized the effect of TFE on this peptide experimentally by ECD spectroscopy. Our TFE model in question reproduced the helix-promoting effect of TFE and provided insight into the mechanisms of TFE action on peptides. Our simulations confirmed the preferential interaction of TFE molecules with alpha-helices, although the TFE molecules accumulate in the vicinity of the peptides in various conformations. Moreover, we observed a significant effect of TFE on the thermodynamics of the helix-coil transition and a change in local conformational preferences in the unfolded (coil) state induced by TFE. In addition, our simulation-based analysis suggests that different mechanisms participate in helix stabilization in both model peptides in water and TFE solution. Our results thus support the picture of complex TFE action on peptides that is further diversified by the identity and intrinsic properties of the peptide.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

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Project

<a href="/en/project/LM2015047" target="_blank" >LM2015047: Czech National Infrastructure for Biological Data</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

—

Volume of the periodical

120

Issue of the periodical within the volume

6

Country of publishing house

US - UNITED STATES

Number of pages

12

Pages from-to

1048-1059

UT code for WoS article

000370678500002

EID of the result in the Scopus database

2-s2.0-84959421420