2009
DOI: 10.1248/cpb.57.481
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Interaction of DNA Minor Groove Binder Hoechst 33258 with Bovine Serum Albumin

Abstract: . The CD spectrum of BSA revealed that the binding of Hoechst 33258 to BSA causes loss in the secondary structure but increases the thermal stability of the protein. The results indicated that hydrophobic interactions were the predominant intermolecular forces in stabilizing BSA-Hoechst 33258 complex. The possible implications of these results will be on designing better therapeutic minor groove binding drug molecules.

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Cited by 47 publications
(23 citation statements)
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References 43 publications
(41 reference statements)
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“…Although high glass transition temperatures would keep the vaccine more stable during storage, replacing PVP by BSA enhanced vaccine virus stability (Table 1). Probably other stabilizing mechanisms such as hydrophobic interaction of BSA [22][23][24] with the enveloped ND vaccine were responsible for the vaccine storage stability, while PVP can only engage in hydrophilic interactions [25].…”
Section: Discussionmentioning
confidence: 99%
“…Although high glass transition temperatures would keep the vaccine more stable during storage, replacing PVP by BSA enhanced vaccine virus stability (Table 1). Probably other stabilizing mechanisms such as hydrophobic interaction of BSA [22][23][24] with the enveloped ND vaccine were responsible for the vaccine storage stability, while PVP can only engage in hydrophilic interactions [25].…”
Section: Discussionmentioning
confidence: 99%
“…Thus, letting tumor cells to apoptosis is a requirement for an anticancer agent. It is generally accepted that cytotoxic drugs eliminate malignant cells by inducing apoptosis 32,33 . The activation of caspases, a family of important signaling molecules with various tasks depending on subtype and organ, is a marker for apoptosis 34 .…”
Section: Analysis Of Caspase-3 Activationmentioning
confidence: 99%
“…Dacarbazine, an imidazole compound, inhibits DNA, RNA and protein synthesis by alkylation mechanism 31 . Bisbenzimidazole compounds such as Hoechst 33342 and Hoechst 33258 have anticancer ability to inhibit DNA topoisomerase I and many other cellular processes 32 . Natural bis(benzoxazole) product UK-11 shows cytotoxic action on cancer cells, selectively 33 .…”
Section: Introductionmentioning
confidence: 99%
“…HSA has multiple binding sites for lower and higher fatty acids, and there are dedicated binding sites for aromatic compounds. Specific binding sites named Sudlow I and II are characterized by their binding of aromatic compounds . The amino acid sequence of HSA contains 17 disulfide bridges, one free thiol (Cys34) and a single tryptophan (Trp214), which may be vital when HSA binds with ligands along the chain …”
Section: Introductionmentioning
confidence: 99%
“…In the circulation, the binding process between a particular molecule and serum albumin may impact the structure of HSA. In other words, pathological factors can significantly alter the binding of ligands, and one such pathological condition is excess glucose . As the level of glucose increases, HSA is non‐enzymatically glycated to reduce sugar from blood.…”
Section: Introductionmentioning
confidence: 99%