Self-assembly and molecular dynamics of peptide-functionalized polyphenylene dendrimers
| dc.contributor.author | Mondeshki, M. | en |
| dc.contributor.author | Mihov, G. | en |
| dc.contributor.author | Graf, R. | en |
| dc.contributor.author | Spiess, H. W. | en |
| dc.contributor.author | Mullen, K. | en |
| dc.contributor.author | Papadopoulos, P. | en |
| dc.contributor.author | Gitsas, A. | en |
| dc.contributor.author | Floudas, G. | en |
| dc.date.accessioned | 2015-11-24T18:35:42Z | |
| dc.date.available | 2015-11-24T18:35:42Z | |
| dc.identifier.issn | 0024-9297 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/17126 | |
| dc.rights | Default Licence | - |
| dc.subject | electric dipole moment | en |
| dc.subject | alpha-helix | en |
| dc.subject | polypeptide solutions | en |
| dc.subject | dielectric properties | en |
| dc.subject | triblock copolymers | en |
| dc.subject | dendritic polymers | en |
| dc.subject | solid polypeptides | en |
| dc.subject | l-lysine | en |
| dc.subject | poly(l-lysine) | en |
| dc.subject | shape | en |
| dc.title | Self-assembly and molecular dynamics of peptide-functionalized polyphenylene dendrimers | en |
| heal.abstract | The self-assembly mechanism and the associated molecular dynamics are studied for a series of poly-L-lysine-functionalized polyphenylene dendrimer melts as a function of the core size (generation), functionality, and polypeptide length using X-rays, solid-state NMR, calorimetry, and dielectric spectroscopy. A striking dependence of the polyphenylene self-assembly on the poly-L-lysine length is shown. In addition, the type (alpha-helix/beta-sheet) of peptide secondary structure is controlled by the packing restrictions imposed by the polyphenylene core. We show that constrained poly-L-lysines can adopt different secondary structures from their linear analogues. The dynamic investigation revealed significant mobility associated solely with the polypeptide through three processes: a glass transition, a slower process associated with the relaxation of alpha-helical segments, and a glassy mode whose origin could be resolved by site-specific solid-state NMR techniques. Solid-state NMR studies further indicated a mobility gradient in going from the rigid peptide backbone to the side chains. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1021/Ma0621270 | - |
| heal.identifier.secondary | <Go to ISI>://000242935400094 | - |
| heal.identifier.secondary | http://pubs.acs.org/doi/pdfplus/10.1021/ma0621270 | - |
| heal.journalName | Macromolecules | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2006 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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