Aggregation Characteristics of Biobased Anionic Surfactant, Hydroxy Alkane Sulfonate in Aqueous CaCl Solutions: Vesicle and Supported Bilayer Formation.

Vesicles are known to spontaneously adsorb onto solid-liquid interfaces and to form supported bilayers in aqueous solution. Cationic surfactants have typically been used to generate supported bilayers because solid surfaces in water are often negatively charged. The present study investigated the aggregation behavior of an anionic surfactant, hydroxy alkane sulfonate having a C18 alkyl chain (C18HAS) in aqueous CaCl solutions.

Molecular design, chemical synthesis, and biological evaluation of agents that selectively photo-degrade the transcription factor estrogen receptor-α.

2-Phenylquinoline (1) degraded proteins under photo-irradiation with long-wavelength UV light without additives and under neutral conditions. We designed and synthesized a 2-phenylquinoline-estrogen receptor-α (ER-α) agonist (hybrid 2) and a 2-phenylquinoline-ER-α antagonist (hybrid 3) containing estradiol and 4-hydroxytamoxifen moieties, respectively. These 2-phenylquinoline hybrids effectively and selectively photo-degraded the target transcription factor, ER-α, which has a high affinity for estradiol and 4-hydroxytamoxifen.

Target-selective degradation of cancer-related proteins by novel photosensitizers for molecular-targeted photodynamic therapy.

Proteins are key players in many biological events including cancers. The development of novel photosensitizers for the selective degradation of cancer-related proteins has attracted much attention in the fields of photodynamic therapy for various cancers. In this review article, several novel photosensitizers, which selectively degrade cancer-related proteins under photoirradiation and mild conditions without any further additives, are introduced.

Target-selective degradation of proteins by a light-activated 2-phenylquinoline-estradiol hybrid.

A designed 2-phenylquinoline-estradiol hybrid effectively and selectively degraded the target transcription factor, human estrogen receptor-alpha (hER-alpha), which has a high affinity with the estradiol moiety, under long-wavelength UV photo-irradiation, without additives and under neutral conditions.