Linked Life Data

21214221

Source:http://linkedlifedata.com/resource/pubmed/id/21214221

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-3-25
pubmed:abstractText
Our rigorous re-examination of the conformational properties of bastadins that comprise the isobastarane and bastarane-type macrocycle has generated some interesting new insights. We determined that these macrocycles are flexible and possess a surprising degree of reflection symmetry that generates enantiomeric conformations. The macrocycle symmetry arises from its ability to twist in a disrotatory fashion, providing one set of conformers, and then twists with the opposite disrotation to generate a corresponding set of enantiomers. Overall, the isobastarane conformations for (E,E)-bastadin 19 (1a) are complex and can access several distinct ring conformations. In contrast, the bastarane macrocycle in bastadin 5 (2) and bastadin 6 (3) maintains a similar overall shape. We postulate that the short-term stability of the (Z)-oximo amide, an uncommon configuration found in bastadins and psammaplins, is due to the existence of conformers with intramolecular hydrogen bonds involving the (Z)-oxime, and hydrogen bonding impedes oxime isomerization to the more stable (E)-oximo amide in solution. Finally, the modeling results provided insights toward understanding the different antiproliferative activity against endothelial cells as well as Ca(2+) channel modulation activities attributed to bastaranes 2 and 3 versus isobastarane 1a.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1520-6025
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
402-10
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Unraveling the bastarane and isobastarane oximo amide configurations and associated macrocycle conformations: implications of their influence on bioactivities.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States. winman@ucsc.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural