Biotin-decorated anti-cancer nucleotide theranostic conjugate of human serum albumin: Where the seed meets the soil?. Issue 3 (1st February 2018)

• Record Type: Journal Article
• Authors: Popova, Tatyana V.; Khan, Hamda; Chubarov, Alexey S.; Lisitskiy, Vladimir A.; Antonova, Natalya M.; Akulov, Andrey E.; Shevelev, Oleg B.; Zavjalov, Evgenii L.; Silnikov, Vladimir N.; Ahmad, Saheem; Godovikova, Tatyana S.
• Is Part Of: Bioorganic & medicinal chemistry letters. Volume 28:Issue 3(2018)
• Page Start: 260
• Page End: 264
• Publication Date: 2018-02-01
• Subjects: Bio biotin -- HSA human serum albumin -- Hcy homocysteine -- Hcy-HSA N-homocysteinylated human serum albumin -- HTL homocysteine thiolactone -- MI maleimide -- MRI magnetic resonance imaging -- PEG poly(ethylene glycol) -- PEGBio biotin functionalized poly(ethylene glycol) -- PFT perfluorotoluene -- PFT-HTL N-(2, 3, 5, 6-tetrafluoro-4-(trifluoromethyl)phenyl)homocysteine thiolactone -- TFT 5-trifluoromethyl-2′-deoxyuridine (trifluorothymidine); Biotinylated albumin conjugate -- Dual-labeled human serum albumin -- Trifluorothymidine theranostic conjugate -- Fluorescence-based molecular imaging -- Anti-tumor activity; Bioorganic chemistry -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1016/j.bmcl.2017.12.061
• Languages: English
• ISSNs: 0960-894X

Abstract

Graphical abstract: Abstract: Human serum albumin is playing an increasing role as a drug carrier in clinical settings. Biotin molecules are often used as suitable tags in targeted anti-tumor drug delivery systems. We report on the synthesis and properties of a new multimodal theranostic conjugate based on an anti-cancer fluorinated nucleotide conjugated with a biotinylated dual-labeled albumin. Interestingly, in vitro and in vivo study revealed stronger anti-tumor activity of the non-tagged theranostic conjugate than that of the biotin-tagged conjugate, which can be explained by decreased binding of the biotin-tagged conjugate to cellular receptors. Our study sheds light on the importance of site-specific albumin modification for the design of albumin-based drugs with desirable pharmaceutical properties.