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Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy

Andrey Vasil'evich Filippov 1, 2
Andrey Vasil'evich Filippov
, 
Aidar Masgutovich Khakimov 1
Aidar Masgutovich Khakimov
, 
Sergii Afonin 3
Sergii Afonin
, 
Oleg Nikolaevich Antzutkin 2, 4
Oleg Nikolaevich Antzutkin
10.1016/j.mencom.2013.11.002
Published 2013-10-30
Communication , Volume 23, Issue 6, 313-315
6
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Filippov A. V. et al. Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy // Mendeleev Communications. 2013. Vol. 23. No. 6. pp. 313-315.
GOST all authors (up to 50) Copy
Filippov A. V., Khakimov A. M., Afonin S., Antzutkin O. N. Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy // Mendeleev Communications. 2013. Vol. 23. No. 6. pp. 313-315.
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TY - JOUR
DO - 10.1016/j.mencom.2013.11.002
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2013.11.002
TI - Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy
T2 - Mendeleev Communications
AU - Filippov, Andrey Vasil'evich
AU - Khakimov, Aidar Masgutovich
AU - Afonin, Sergii
AU - Antzutkin, Oleg Nikolaevich
PY - 2013
DA - 2013/10/30
PB - Mendeleev Communications
SP - 313-315
IS - 6
VL - 23
ER -
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@article{2013_Filippov,
author = {Andrey Vasil'evich Filippov and Aidar Masgutovich Khakimov and Sergii Afonin and Oleg Nikolaevich Antzutkin},
title = {Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy},
journal = {Mendeleev Communications},
year = {2013},
volume = {23},
publisher = {Mendeleev Communications},
month = {Oct},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2013.11.002},
number = {6},
pages = {313--315},
doi = {10.1016/j.mencom.2013.11.002}
}
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Filippov, Andrey Vasil'evich, et al. “Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy.” Mendeleev Communications, vol. 23, no. 6, Oct. 2013, pp. 313-315. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2013.11.002.

Abstract

The effects of five fragments of prostatic acid phosphatase on dimyristoylphosphatidylcholine lipid multi-lamellar liposomes were studied by 2H and 31P NMR spectroscopy and those on planar supported multi-bilayers of the same lipid, by 1H and 31P NMR spectro-scopy. It was found that hydrophobic interaction is a dominated factor of the peptide–membrane binding, while the short α-helical fragments PAP(262-270) and PAP(262-272) strongly interact with the membrane at the interface, generally following to the Gibbs free energy of water-to-interface insertion.

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