Effect of macrocyclic compounds to protein aggregation

When studying the affinity of albumin to low molecular weight compounds, an extremely interesting phenomenon was discovered. Some porphyrins and macrocyclic compounds intercalate into the serum albumin blood globule, which leads to an increase in the proportion of β-folding and subsequent protein ag...

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Bibliographic Details
Published in:Journal of inclusion phenomena and macrocyclic chemistry 2019, Vol.95 (3-4), p.199-206
Main Authors: Lebedeva, Natalia Sh, Yurina, Elena S., Gubarev, Yury A., Koifman, Oskar I.
Format: Article
Language:English
Subjects:
Agglomeration
Chemistry
Chemistry and Materials Science
Crystallography and Scattering Methods
Food Science
Low molecular weights
Macrocyclic compounds
Organic Chemistry
Porphyrins
Proteins
Review Article
Serum albumin
Zeta potential
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Summary:When studying the affinity of albumin to low molecular weight compounds, an extremely interesting phenomenon was discovered. Some porphyrins and macrocyclic compounds intercalate into the serum albumin blood globule, which leads to an increase in the proportion of β-folding and subsequent protein aggregation. Is it possible that organic molecules, getting into the protein globule, cause a local conformational alpha–beta transition and change the zeta potential of the globule, which later leads to aggregation? We tried to answer this and other questions in this review, based on our own and literary information.
ISSN:1388-3127
1573-1111
DOI:10.1007/s10847-019-00947-1