Linked Life Data

19200035

Source:http://linkedlifedata.com/resource/pubmed/id/19200035

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-2-9
pubmed:abstractText
A novel neuroprotective peptide, Humanin (HN), has a strong tendency to aggregate in phosphate-buffered saline. Here we attempted to reduce aggregation employing an aqueous phosphate solution, without NaCl, at pH 6.0 and low peptide concentrations wherever possible. Such a condition, though not fully physiological, allowed us to determine the secondary structure and molecular weight of the peptides. Comparison of a parent HN peptide, an inactive analog (S7A-HN) and a 1000-fold more active analog (S14G-HN) showed no apparent differences in the secondary structure. These peptides were all disordered over the wide range of peptide concentration. Sedimentation analysis was done only for HN and S7A-HN and showed aggregation into soluble oligomers in 20 mM phosphate at pH 6.0. Aggregation was greatly suppressed in 5 mM phosphate at the same pH in terms of aggregate size, with the formation of smaller oligomers. Sedimentation velocity experiments at 60,000 rpm in 5 mM phosphate at pH 6.0 showed that both HN and S7A-HN distributed into soluble aggregates that sedimented to the bottom of the cell and low molecular weight species that approached sedimentation equilibrium. The mass of this low molecular weight species was determined by sedimentation equilibrium to be close to monomers for both peptides. Thus, these results clearly demonstrate that the active HN and inactive S7A-HN are identical in structure and hence there is no apparent correlation between solution structure and biological activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0929-8665
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
132-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Active form of neuroprotective Humanin, HN, and inactive analog, S7A-HN, are monomeric and disordered in aqueous phosphate solution at pH 6.0; No correlation of solution structure with activity.
pubmed:affiliation
Department of Molecular Bioprocessing, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article