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Photodynamic Inactivation of Gramicidin Channels in Bilayer Lipid Membranes: Protective Efficacy of Singlet Oxygen Quenchers Depends on Photosensitizer Location

T. I. Rokitskaya*, A. M. Firsov, E. A. Kotova, and Y. N. Antonenko

Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, 119991 Moscow, Russia; fax: +7 (495) 939-3181; E-mail: rokitskaya@genebee.msu.ru

* To whom correspondence should be addressed.

Received December 23, 2014; Revision received February 27, 2015
The impact of double bonds in fatty acyl tails of unsaturated lipids on the photodynamic inactivation of ion channels formed by the pentadecapeptide gramicidin A in a planar bilayer lipid membrane was studied. The presence of unsaturated acyl tails protected gramicidin A against photodynamic inactivation, with efficacy depending on the depth of a photosensitizer in the membrane. The protective effect of double bonds was maximal with membrane-embedded chlorin e6-monoethylenediamine monoamide dimethyl ester, and minimal – in the case of water-soluble tri-sulfonated aluminum phthalocyanine (AlPcS3) known to reside at the membrane surface. By contrast, the protective effect of the hydrophilic singlet oxygen scavenger ascorbate was maximal for AlPcS3 and minimal for amide of chlorin e6 dimethyl ester. The depth of photosensitizer position in the lipid bilayer was estimated from the quenching of photosensitizer fluorescence by iodide. Thus, the protective effect of a singlet oxygen scavenger against photodynamic inactivation of the membrane-inserted peptide is enhanced upon location of the photosensitizer and scavenger molecules in close vicinity to each other.
KEY WORDS: photodynamic action, gramicidin A, photosensitizer, unsaturated lipids, ascorbate, singlet oxygen, bilayer lipid membrane

DOI: 10.1134/S0006297915060097