Linked Life Data

2337975

Source:http://linkedlifedata.com/resource/pubmed/id/2337975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1990-6-20
pubmed:abstractText
The effects of homopolymeric amino acids (molecular weight 2300 to 14,000) on the surface activity of dipalmitoyl phosphatidylcholine (DPPC) and DPPC/egg-phosphatidylglycerol (PG) were characterized by adsorption and dynamic surface tension lowering measurements at 37 degrees C. Homopolyamino acids studied included poly-L-leucine (poly-Leu) and poly-L-valine (poly-Val), since Leu and Val are known to be prominent in the structure of hydrophobic lung surfactant apoprotein SP-B and SP-C. In addition, several other homopolyamino acids with varying hydrophobicity index were also investigated, including poly-L-phenylalanine (poly-Phe), poly-L-serine (poly-Ser), poly-L-lysine (poly-Lys) and poly-L-glutamic acid (poly-Glu). Results showed that hydrophobic poly-Leu and poly-Phe at 1 and 10 weight percent greatly increased the adsorption facility of DPPC and DPPC/PG mixtures, with maximum surface pressures (up to 49 mN/m) near the equilibrium limit for phospholipid systems. In oscillating bubble studies, 1% mixture of poly-Leu or poly-Phe with DPPC or 8:2 DPPC/PG lowered surface tension into the range (near 1 mN/m) associated with active lung surfactant. In contrast, mixtures of DPPC and DPPC/PG with the more hydrophilic peptides poly-Ser, poly-Lys and poly-Glu showed little or no enhancement of surface activity over the phospholipids alone. Mixtures of poly-Val and phospholipids did not combine well with the simple co-sonication procedure used, and also exhibited little improvement in surface activity.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0009-3084
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-64
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Hydrophobic homopolymeric peptides enhance the biophysical activity of synthetic lung phospholipids.
pubmed:affiliation
Department of Pediatrics, University of Rochester, New York 14642.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't