Source:http://linkedlifedata.com/resource/pubmed/id/17518440
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2007-6-11
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pubmed:abstractText |
An underwater bioadhesive generally comprises a multiprotein complex that provides a molecular basis for self-assembly. We report here a new class of self-assembling peptide inspired by a 20 kDa barnacle cement protein. Studies on the chemically synthesized 24-residue peptide have revealed that (1) it underwent irreversible self-assembly upon the addition of salt, (2) the self-assembly was started at a salt concentration close to that of seawater with noncovalent intermolecular interactions, (3) the self-assembled material resembled a macroscopic membrane of interwoven nanofilaments, (4) incubation in an alkaline pH range formed the intramolecular disulfide bond of a peptide molecule, thus triggering a conformation change of the molecule, and (5) conformational change of the building block promoted the formation of a nanofiber, resulting in the display of a three-dimensional meshlike mesoscopic structure with defined pores having a diameter of approximately 200 nm. The peptide is likely to provide a suitable basis for further development of peptide-based materials.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesives,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salts
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1525-7797
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1830-5
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pubmed:meshHeading |
pubmed-meshheading:17518440-Adhesiveness,
pubmed-meshheading:17518440-Adhesives,
pubmed-meshheading:17518440-Animals,
pubmed-meshheading:17518440-Circular Dichroism,
pubmed-meshheading:17518440-Cysteine,
pubmed-meshheading:17518440-Hydrogen-Ion Concentration,
pubmed-meshheading:17518440-Microscopy, Atomic Force,
pubmed-meshheading:17518440-Microscopy, Electron, Scanning,
pubmed-meshheading:17518440-Molecular Conformation,
pubmed-meshheading:17518440-Peptides,
pubmed-meshheading:17518440-Protein Folding,
pubmed-meshheading:17518440-Protein Structure, Secondary,
pubmed-meshheading:17518440-Proteins,
pubmed-meshheading:17518440-Salts,
pubmed-meshheading:17518440-Thoracica
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pubmed:year |
2007
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pubmed:articleTitle |
Self-assembling peptide inspired by a barnacle underwater adhesive protein.
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pubmed:affiliation |
Marine Biotechnology Institute, 3-75-1 Heita, Kamaishi, Iwate 026-0001, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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