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Chiral recognition of bilirubin and biliverdin in liposomes and micelles
P. Novotná, F. Králík, M. Urbanová,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- biliverdin chemie metabolismus MeSH
- cholesterol analogy a deriváty metabolismus MeSH
- kompetitivní vazba MeSH
- kyseliny cholové metabolismus MeSH
- lidé MeSH
- micely * MeSH
- molekulární konformace MeSH
- molekulární modely MeSH
- sérový albumin hovězí metabolismus MeSH
- skot MeSH
- stereoizomerie MeSH
- unilamelární lipozómy chemie metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The structural formula of biologically important chiral pigments bilirubin and biliverdin differs only by one double bond. We showed that this results in dissimilar interactions with two models of membranes: cationic liposomes composed of 3β-[N-(N',N'-dimethylaminoethane)-carbamoyl]cholesterol and zwitterionic micelles from 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). While the liposomes recognized the P-form of bilirubin, the micelles recognized its M-form. Both recognized the P-form of biliverdin. Our study also comprised ternary systems consisting of the pigments, model membranes and serum albumin (human and bovine). Bilirubin preferentially interacted with the albumins even in the presence of the liposomes. On the other hand, biliverdin preferred the liposomes. Remarkably, the presence of CHAPS completely changed the biliverdin binding to the protein. Because our study was oriented on different chiral interactions, a chiroptical method of electronic circular dichroism was chosen as the principal method to study our systems. As complementary methods, UV-vis absorption and fluorescence emission were used.
Citace poskytuje Crossref.org
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- $a The structural formula of biologically important chiral pigments bilirubin and biliverdin differs only by one double bond. We showed that this results in dissimilar interactions with two models of membranes: cationic liposomes composed of 3β-[N-(N',N'-dimethylaminoethane)-carbamoyl]cholesterol and zwitterionic micelles from 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). While the liposomes recognized the P-form of bilirubin, the micelles recognized its M-form. Both recognized the P-form of biliverdin. Our study also comprised ternary systems consisting of the pigments, model membranes and serum albumin (human and bovine). Bilirubin preferentially interacted with the albumins even in the presence of the liposomes. On the other hand, biliverdin preferred the liposomes. Remarkably, the presence of CHAPS completely changed the biliverdin binding to the protein. Because our study was oriented on different chiral interactions, a chiroptical method of electronic circular dichroism was chosen as the principal method to study our systems. As complementary methods, UV-vis absorption and fluorescence emission were used.
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