Linked Life Data

6767029

Source:http://linkedlifedata.com/resource/pubmed/id/6767029

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-5-14
pubmed:abstractText
Analogues of the carboxyl protease inhibitor, pepstatin, were synthesized from optically pure forms of N-(tert-butoxycarbonyl)-4-amino-3-hydroxy-6-methylheptanoic acid (Boc-Sta), and the inhibition of pepsin and renin was determined. In addition, the new amino acid (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid [AHPPA] was synthesized and the stereochemistry of the 3 and 4 positions established. The tripeptides isovaleryl-L-valyl-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoyl-L-alanine isoamylamide [Iva-Val-(3S,4S)-Sta-Ala-NHiC5H11] and Iva-Val-(3S,4S)-AHPPA-Ala-NHiC5H11 were found to be potent inhibitors of pepsin with Ki = 1 x 10(-9) and 0.9 x 10(-9) M, respectively. Changing the chirality of the (3S)-hydroxy group to 3R or shortening the peptide chain diminished binding to pepsin over 100-fold. Three structural requirements necessary for potent inhibition of pepsin are proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Synthesis of analogues of the carboxyl protease inhibitor pepstatin. Effects of structure on inhibition of pepsin and renin.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.