Chirality and helix stability of polyglutamic acid enantiomers
| dc.contributor.author | Kodona, E. K. | en |
| dc.contributor.author | Alexopoulos, C. | en |
| dc.contributor.author | Panou-Pomonis, E. | en |
| dc.contributor.author | Pomonis, P. J. | en |
| dc.date.accessioned | 2015-11-24T16:53:47Z | |
| dc.date.available | 2015-11-24T16:53:47Z | |
| dc.identifier.issn | 0021-9797 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10066 | |
| dc.rights | Default Licence | - |
| dc.subject | ordered micellar aggregates | en |
| dc.subject | poly-l-glutamic acid | en |
| dc.subject | poly-d-glutamic acid | en |
| dc.subject | c(14)tab | en |
| dc.subject | thermal stability | en |
| dc.subject | chirality | en |
| dc.subject | amino-acids | en |
| dc.subject | mesoporous silica | en |
| dc.subject | amphipathic peptides | en |
| dc.subject | racemic mixtures | en |
| dc.subject | alpha-helix | en |
| dc.subject | proteins | en |
| dc.subject | water | en |
| dc.subject | transition | en |
| dc.subject | design | en |
| dc.subject | conformation | en |
| dc.title | Chirality and helix stability of polyglutamic acid enantiomers | en |
| heal.abstract | In this work the chirality and the relative thermal stability of ordered micellar aggregates of poly-L- and poly-D-glutamic acids with the cationic surfactant C(14)TAB is examined. The complexed mesophases poly-L-Glu/C(14)TAB and poly-D-Glu/C-14 TAB were characterized by circular dichroism (CD) in the temperature range 10-70 degrees C for their chirality and thermal stability as well as by X-ray diffraction (XRD) for the micellar ordered structure. Low angle XRD analysis showed that both micellar aggregates poly-L-Glu/C(14)TAB and poly-D-Glu/C(14)TAB are hexagonally packed in a MCM-41 fashion with an intermicellar distance identical and equal to 3.55 +/- 0.10 nm. The CID spectra indicated that both complexes poly-L-Glu/C(14)TAB and poly-D-Glu/C(14)TAB possess a mainly alpha-helix structure and are exact mirror images to each other. The same mirror images and a mainly a-helix configuration were also observed by CID for the free poly-L- and poly-D-glutamic acids at room temperature. As the temperature increases from 10 up to 70 degrees C the ce-helix of the poly-L-glutamic acid is gradually transformed to a mixture containing increased amounts of the 3(10)-helix while the alpha-helix structure of the poly-D-glutamic acid is constantly degenerated. In contrast the alpha-helices of the corresponding complexes poly-L-Glu/C(14)TAB and poly-D-Glu/C(14)TAB are degenerated upon heating without appreciable increase of the 3(10)-helices as an intermediate configuration. This difference in helix conservation is attributed to increase protection of the L-enantiomers, compared to D-enantiomers, which might be related to the survival of L-aminoacids in the living world. (c) 2007 Elsevier Inc. All rights reserved. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | DOI 10.1016/j.jcis.2007.10.063 | - |
| heal.identifier.secondary | <Go to ISI>://000252750400011 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0021979707016098/1-s2.0-S0021979707016098-main.pdf?_tid=996fa3fd02ec66aef7ece443fbd22d65&acdnat=1333036361_8b537f9caa843d7030110687b21f77f8 | - |
| heal.journalName | J Colloid Interface Sci | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2008 | - |
| heal.publisher | Elsevier | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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