S. doi:10.1371/journal.pone.0049226.gThe crucial requirement for O2(1Dg)-mediated

S. doi:10.1371/journal.pone.0049226.gThe crucial requirement for O2(1Dg)-mediated protein damage to occur efficiently is localization of amino acid residues sensitive to O2(1Dg) on the surface of compact capsid structures. The crystal structures of MPyV and Simian virus 40 (SV40) have been determined. The capsid shell of the polyomavirus used in this study is composed of 72 pentamers of the major structural protein VP1 (Fig. 9). Two other minor structural proteins, VP2 and VP3, are not exposed on surface of the capsid. VP1 from both polyomaviruses contains a b-sandwich core with several outfacing loops [38,39]. These interactive loops are exposed on the surface of VP1 pentamers and polyomavirus capsids. Computer analysis revealed the presence of several tyrosine and tryptophan residues as well as one histidine and one methionine residue in the surface loops. Many other sensitive 23727046 amino acid residues occurring in the VP1 b-sandwich core might be less accessible. The level of accessibility of the amino acid residues that are sensitive to O2(1Dg) can differ among capsid proteins of nonenveloped viruses, and it will be necessary to test the efficiency of their inactivation individually. Recently, efficient inactivation of the non-enveloped bacteriophage MS-2 by visible light was reported based on using a cationic fullerene derivative with amine functionality as a photosensitizer to produce O2(1Dg) [40]. Based on the computer analysis of capsid subunits from viruses with known tertiary structures, we predict that human papillomaviruses or poliovirus can be efficiently inactivated by O2(1Dg) produced by the photosensitizer used in this study. Thus, the photosensitizersimmobilized on the nanofibers can be highly useful for the development of novel approaches for inactivating both enveloped and non-enveloped viruses.ConclusionsThis study, addressing the photophysical, photochemical and photovirucidal properties of MedChemExpress SR 3029 polymer nanofibers based on the TecophilicH thermoplastic polyurethane and polycaprolactone with an encapsulated 5,10,5,20-tetraphenylporphyrin photosensitizer, reveals that these textiles are efficient sources of short-lived virucidal O2(1Dg). The photoproduction and lifetime of O2(1Dg) in these 301-00-8 Materials are sufficient to exert strong photovirucidal effects on non-enveloped polyomaviruses and enveloped baculoviruses on the surface of the nanofiber textiles. These new nanomaterials could be considered for use in a number of medical applications and for the development of O2(1Dg) inactivation tests for enveloped and non-enveloped viruses.Materials and Methods Chemicals5,10,15,20-tetraphenylporphyrin (TPP), 5,10,15,20-tetrakis(4sulfonatophenyl)porphyrin (TPPS), 9,10-anthracenediyl-bis(methylene)dimalonic acid (AMA) and tetraethylammonium bromide (TEAB) were purchased from Aldrich (USA). Formic acid, acetic acid, N,N-dimethylacetamide (DMAc) and toluene were purchased from Penta (Czech Republic). Polyurethane TecophilicH HP-60D-60, a thermoplastic elastamer consisting of segmented block copolymers and synthesized from 4,49-diisocyanato dicyclohexylmethane, 1,4-butanediol and polyethylene glycol, was purchased from Lubrizol Advanced Materials (USA). Polycaprolactone (MW 70,000) was purchased from Scientific Polymer Products, Inc. (USA). For DNA staining, 4,69-diamidino-2phenylindole, dihydrochloride (DAPI) was purchased from Sigma (USA).Figure 9. Structure of the polyomavirus capsid. Structure of the polyomavirus capsid (C) formed by 72 p.S. doi:10.1371/journal.pone.0049226.gThe crucial requirement for O2(1Dg)-mediated protein damage to occur efficiently is localization of amino acid residues sensitive to O2(1Dg) on the surface of compact capsid structures. The crystal structures of MPyV and Simian virus 40 (SV40) have been determined. The capsid shell of the polyomavirus used in this study is composed of 72 pentamers of the major structural protein VP1 (Fig. 9). Two other minor structural proteins, VP2 and VP3, are not exposed on surface of the capsid. VP1 from both polyomaviruses contains a b-sandwich core with several outfacing loops [38,39]. These interactive loops are exposed on the surface of VP1 pentamers and polyomavirus capsids. Computer analysis revealed the presence of several tyrosine and tryptophan residues as well as one histidine and one methionine residue in the surface loops. Many other sensitive 23727046 amino acid residues occurring in the VP1 b-sandwich core might be less accessible. The level of accessibility of the amino acid residues that are sensitive to O2(1Dg) can differ among capsid proteins of nonenveloped viruses, and it will be necessary to test the efficiency of their inactivation individually. Recently, efficient inactivation of the non-enveloped bacteriophage MS-2 by visible light was reported based on using a cationic fullerene derivative with amine functionality as a photosensitizer to produce O2(1Dg) [40]. Based on the computer analysis of capsid subunits from viruses with known tertiary structures, we predict that human papillomaviruses or poliovirus can be efficiently inactivated by O2(1Dg) produced by the photosensitizer used in this study. Thus, the photosensitizersimmobilized on the nanofibers can be highly useful for the development of novel approaches for inactivating both enveloped and non-enveloped viruses.ConclusionsThis study, addressing the photophysical, photochemical and photovirucidal properties of polymer nanofibers based on the TecophilicH thermoplastic polyurethane and polycaprolactone with an encapsulated 5,10,5,20-tetraphenylporphyrin photosensitizer, reveals that these textiles are efficient sources of short-lived virucidal O2(1Dg). The photoproduction and lifetime of O2(1Dg) in these materials are sufficient to exert strong photovirucidal effects on non-enveloped polyomaviruses and enveloped baculoviruses on the surface of the nanofiber textiles. These new nanomaterials could be considered for use in a number of medical applications and for the development of O2(1Dg) inactivation tests for enveloped and non-enveloped viruses.Materials and Methods Chemicals5,10,15,20-tetraphenylporphyrin (TPP), 5,10,15,20-tetrakis(4sulfonatophenyl)porphyrin (TPPS), 9,10-anthracenediyl-bis(methylene)dimalonic acid (AMA) and tetraethylammonium bromide (TEAB) were purchased from Aldrich (USA). Formic acid, acetic acid, N,N-dimethylacetamide (DMAc) and toluene were purchased from Penta (Czech Republic). Polyurethane TecophilicH HP-60D-60, a thermoplastic elastamer consisting of segmented block copolymers and synthesized from 4,49-diisocyanato dicyclohexylmethane, 1,4-butanediol and polyethylene glycol, was purchased from Lubrizol Advanced Materials (USA). Polycaprolactone (MW 70,000) was purchased from Scientific Polymer Products, Inc. (USA). For DNA staining, 4,69-diamidino-2phenylindole, dihydrochloride (DAPI) was purchased from Sigma (USA).Figure 9. Structure of the polyomavirus capsid. Structure of the polyomavirus capsid (C) formed by 72 p.

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