Linked Life Data

16185864

Source:http://linkedlifedata.com/resource/pubmed/id/16185864

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2005-10-19
pubmed:abstractText
Collagen is acknowledged as one of the most prominent biomaterials on account of its high biocompatibility and biostability. The development of artificial collagens to replace the animal-derived collagens presents a challenge in the formation of safer and highly functionalized biomaterials. Here, a novel peptide-based system for obtaining collagen-like supramolecules via a spontaneous self-assembling process is described. The designed collagen-like peptides are self-complementary trimers in which each of the 24-mer peptide strands is tethered by two cystine knots forming a staggered arrangement. Their self-assembling ability in aqueous solution was analyzed by circular dichroism, ultrafiltration, and laser diffraction particle size estimation. The obtained results indicate that the staggered trimers form large supramolecular architectures through intermolecular triple helix-formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5230-3
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Self-complementary peptides for the formation of collagen-like triple helical supramolecules.
pubmed:affiliation
Faculty of Pharmaceutical Science, Niigata University of Pharmacy and Applied Life Sciences, Niigata 950-2081, Japan. koi@niigata-pharm.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't