| Autor: |
Ribeiro, Amélia Galdino, Alves, Josival Emanuel Ferreira, Soares, José Cleberson Santos, dos Santos, Keriolaine Lima, Jacob, Íris Trindade Tenório, da Silva Ferreira, Cindy Juliane, dos Santos, Jéssica Celerino, de Azevedo, Rafael David Souto, de Almeida, Sinara Mônica Vitalino, de Lima, Maria do Carmo Alves |
| Zdroj: |
Medicinal Chemistry Research; Aug2021, Vol. 30 Issue 8, p1469-1495, 27p |
| Abstrakt: |
Albumin is an abundant protein in nature with several biological functions. In the human body, both in health and in illness, its transport function is highlighted by the binding to medicinal drugs and consequent distribution in the bloodstream to the site of action. This is particularly relevant for anticancer treatments, since this protein accumulates in the tumor microenvironment to supply the energetic demands of cancer cells. Different spectroscopy, thermodynamic and in silico studies techniques can be employed to verify how albumin binds to ligands by using either human serum albumin (HSA) or bovine serum albumin (BSA) due to their structural similarity. There is an increasing tendency to use albumin in analyses of absorption, distribution, metabolism and excretion (ADME) properties of anticancer molecules, which further demonstrated the promising character of this investigation for proposing new drugs. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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