Linked Life Data

16718679

Source:http://linkedlifedata.com/resource/pubmed/id/16718679

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-8-31
pubmed:abstractText
Ovalbumin and lysozyme are two main proteins in hen egg white with the isoelectric points of 4.8 and 11, respectively. Herein we report the manufacture of stable, narrowly distributed nanogels (hydrodynamic radius about 100 nm) using a novel and convenient method: ovalbumin and lysozyme solutions were mixed at pH 5.3, the mixture solution was adjusted to pH 10.3, then subsequently stirred and heated. The nanogels were characterized using a combination of techniques. The nanogels have spherical shape and core-shell structure. The core is mainly composed of lysozyme and the shell is mainly composed of ovalbumin. The proteins in the nanogels are in denatured states and they are bound by intermolecular hydrophobic interactions, hydrogen bonds, and disulfide bonds. The charges of the nanogels can be modulated by the pH of the medium. The electrostatic repulsion of ovalbumin molecules on the nanogel surface stabilizes the nanogels in aqueous solution. The formation mechanism of the nanogels is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2006 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
148-58
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Nanogels prepared by self-assembly of oppositely charged globular proteins.
pubmed:affiliation
The Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200433, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't