Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-10-18
pubmed:abstractText
Cyclophilin A, a peptidyl-prolyl cis-trans is isomerase that catalyzes the otherwise slow isomerization of Xaa-Pro imidic bond, specifically binds the immunosuppressant cyclosporin A. Herein we report evidence on binding of cyclolinopeptide A and its synthetic analogue, [Aib5,6-D-Ala8]cyclolinopeptide, to bovine cyclophilin A. Binding experiments were monitored by fluorescence, CD, and second-derivative spectroscopies, evidencing no remarkable rearrangement of protein structure organization. The possibility that cyclolinopeptide A could act as a substitute of cyclosporin A in the immunosuppression modulation is also briefly discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-81
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed-meshheading:7669915-Amino Acid Isomerases, pubmed-meshheading:7669915-Animals, pubmed-meshheading:7669915-Carrier Proteins, pubmed-meshheading:7669915-Cattle, pubmed-meshheading:7669915-Chromatography, Affinity, pubmed-meshheading:7669915-Chromatography, Gel, pubmed-meshheading:7669915-Circular Dichroism, pubmed-meshheading:7669915-Cyclosporine, pubmed-meshheading:7669915-Immunosuppression, pubmed-meshheading:7669915-Kinetics, pubmed-meshheading:7669915-Peptide Fragments, pubmed-meshheading:7669915-Peptides, Cyclic, pubmed-meshheading:7669915-Peptidylprolyl Isomerase, pubmed-meshheading:7669915-Protein Binding, pubmed-meshheading:7669915-Protein Conformation, pubmed-meshheading:7669915-Spectrometry, Fluorescence, pubmed-meshheading:7669915-Spectrophotometry, pubmed-meshheading:7669915-Thymus Gland
pubmed:year
1995
pubmed:articleTitle
Specific interaction between cyclophilin and cyclic peptides.
pubmed:affiliation
Centro Interdipartimentale di Ricerca sui Peptidi Bioattivi and CEINGE-Biotecnologie, Napoli, Italia.
pubmed:publicationType
Journal Article