20566072

Source:http://linkedlifedata.com/resource/pubmed/id/20566072

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0020291, umls-concept:C0030956, umls-concept:C0038280, umls-concept:C0205263, umls-concept:C0205360, umls-concept:C0678594, umls-concept:C1257852
pubmed:issue	8
pubmed:dateCreated	2011-2-7
pubmed:abstractText	The hydrolysis properties of peptide nanospheres consisting of a high-density poly(ethylene glycol) (PEG) brush layer and a poly(L-phenylalanine) (PPhe) core were evaluated in relation to their self-assembled nanostructure. To clarify the effect of the self-assembled structure of the nanospheres on their hydrolysis properties, deformed nanospheres possessing exactly the same components were used as a comparison sample. The desorption of the PEG chains on the peptide nanospheres occurred weakly in alkaline solution at 80° C for 7 days, whereas the deformed nanospheres showed drastic desorption of 70% of the PEG chains within 3 days, possibly due to a low density of PEG chains on their surfaces. The content ratio of the ?-sheet conformation in the core increased with increasing hydrolysis time, suggesting that the ?-helix and random coil conformations were more easily hydrolyzed. Furthermore, the peptide nanospheres retained all their properties, even after autoclaving and ethanol sterilization. These results demonstrated that the self-assembled spherical morphology induced extreme stability and sterilizable peptide nanospheres can be useful as drug-delivery system.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9007393
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Peptides
pubmed:status	MEDLINE
pubmed:issn	1568-5624
pubmed:author	pubmed-author:AkashiMitsuruM, pubmed-author:MatsumotoMasahiroM, pubmed-author:MatsusakiMichiyaM, pubmed-author:WakuTomonoriT
pubmed:issnType	Electronic
pubmed:volume	22
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1035-48
pubmed:meshHeading	pubmed-meshheading:20566072-Hydrolysis, pubmed-meshheading:20566072-Nanospheres, pubmed-meshheading:20566072-Peptides
pubmed:year	2011
pubmed:articleTitle	Self-assembled structure of peptide nanospheres induces high stability against hydrolysis and sterilization.
pubmed:affiliation	Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't