University of Salerno Reports Findings in Eye Proteins (Spectroscopic Investigation of Guest-Guest Interactions in the Nanoporous-Crystalline delta and epsilon Forms of Syndiotactic Polystyrene)
By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Proteins is now available. According to news reporting originating from Fisciano, Italy, by NewsRx correspondents, research stated, "The study of guest-guest interactions in cocrystalline polymer samples is in general complicated by their possible occurrence in both amorphous and crystalline phases. In this paper we show that polarized FTIR spectra of axially oriented films allow discrimination between spatially ordered and disordered guest guest hydrogen bonds occurring in crystalline and amorphous polymer phases, respectively."
Our news editors obtained a quote from the research from the University of Salerno, "In particular, the possible formation of hydrogen bonds between alkyl-esters of para-hydroxybenzoic acid (parabens, relevant antimicrobial molecules), when absorbed in s-PS films exhibiting nanoporous-crystalline monoclinic delta and orthorhombic epsilon phases, has been studied. X-ray diffraction patterns show the formation, for high guest uptake, of triclinic delta and orthorhombic epsilon cocrystalline forms. Infrared linear dichroism measurements show that for delta form films the parabens are present as isolated guests of the cavities of the crystalline form, while guest guest hydrogen bonds between parabens are observed only in the amorphous phase."
According to the news editors, the research concluded: "Analogous measurements for epsilon form films show that, on the contrary, guest guest hydrogen bonds occur prevailingly in the channels of the crystalline phase, with guest molecular planes being roughly parallel to the polymer host helical axes."
For more information on this research see: Spectroscopic Investigation of Guest-Guest Interactions in the Nanoporous-Crystalline delta and epsilon Forms of Syndiotactic Polystyrene. Journal of Physical Chemistry C, 2014;118(22):11774-11783. Journal of Physical Chemistry C can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Journal of Physical Chemistry C - www.pubs.acs.org/journal/jpccck)
The news editors report that additional information may be obtained by contacting A.R. Albunia, University of Salerno, INSTM Res Unit, Dipartimento Chim & Biol, I-84084 Fisciano, SA, Italy (see also Proteins).
Keywords for this news article include: Italy, Gases, Europe, Fisciano, Elements, Hydrogen, Nanoporous, Crystallins, Eye Proteins, Nanotechnology, Inorganic Chemicals, Emerging Technologies
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