Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-10-17
pubmed:abstractText
Successful structural transformations of bioactive compounds into newer skeletal structures by replacing the substructure with others, the features of which are not necessarily similar to but more or less drastically varied from the original one, were proposed to be called being made "bioanalogously" instead of "bioisoterically". Precedents of the bioanalogous replacements of substructures composed of the amide, urea, and related components with others were explored. Anilides, N-phenylureas, and N-phenylcarbamates are bioanalogous as herbicides and topical antiseptics. The bioanalogy can be expanded to include substructures containing ester as well as ether components when local anesthetics are considered together. The polar hydrogen-bonding groups such as (thio)urea, cyanoguanidine, and nitroethenediamine substructures found in histamine H2-receptor antagonists are also bioanalogous in various other bioactive compound series. The open-chain amides and the corresponding "carbonylogously" ring-closured dicarboximides are bioanalogous in agrochemicals and antiandrogens as well as in CNS (central nervous system)-active agents. Very often, similarities in the substructural transformation patterns are observed in various bioanalogous series regardless of differences in the pharmacological category. The observations could be used to predict newer generation structures from an ultimate lead structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
557-66
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Similarities in bioanalogous structural transformation patterns among various bioactive compound series.
pubmed:affiliation
EMIL PROJECT, Fujitsu Kansai Systems Laboratory, Osaka, Japan.
pubmed:publicationType
Journal Article, Review