Taehyung Kim

Polybrominated diphenyl ethers (PBDE) are a class of brominated flame retardants that are recognized as global environmental contaminants with potential adverse effects on human health. This study examined the effects of prenatal exposure to PBDE on reproductive organs, neuronal development, and levels of thyroid hormones. Pregnant rats were exposed to the vehicle or deca-bromodiphenyl ether (BDE) (BDE-209; 5, 40, or 320 mg/kg body weight/d) during gestation days (GD) 6-18. There was a significa

The low stability and fast clearance of tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) are the main obstacles to its implementation as an antitumor agent. Here, we attempted to improve its pharmacokinetic and pharmacodynamic profiles by using PEGylation. N-terminal PEGylated TRAIL (PEG-TRAIL) was synthesized using 2, 5, 10, 20, and 30 kDa PEG. Antitumor effect assessments in HCT116 tumor bearing nude mice showed that all PEG-TRAIL analogues efficiently suppressed mean tumo

This study examined the levels of polybrominated diphenyl ethers (PBDE) in the umbilical cord blood of infants, and investigated the relationship between PBDE concentration and thyroid hormone levels. The concentration of PBDE were measured in the cord blood samples of 108 infants collected in Cheil Woman's Hospital, Seoul, Korea, in 2007. Of 108 pregnant woman reported, the average age was 31.9 +/- 3.54 yr (range 20-42 yr). The mean body weight of the infants was 3.15 +/- 0.57 kg (1.89-4.43 kg)

Dimerization is viewed as the most effective means of increasing receptor binding affinity, and both dimerization and PEGylation effectively prolong the life spans of short-lived peptides and proteins in vivo by delaying excretion via the renal route. Here, we describe the high binding affinities of two long-acting exendin-4 (Ex4) conjugates, dimerized Ex4 (Di-Ex4) and PEGylated Di-Ex-4 (PEG-Di-Ex4). Di-Ex4 and PEG-Di-Ex4 were prepared using cysteine and amine residue specific coupling reactions

The purpose of this study was to optimize an Exendin-4 (Ex4-Cys) site-specific PEGylation method with a high-molecular-weight trimeric PEG. Here, we describe the preparation of C-terminal specific PEGylated Ex4-Cys (C40-tPEG-Ex4-Cys), which was performed using cysteine and amine residue specific coupling reactions between Ex4-Cys and activated trimeric PEG. The C40-PEG-Ex4-Cys was obtained at high yields (~83%) and characterized by MALDI-TOF mass spectrometry. The receptor binding affinity of C4

Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ complex of nitrilotriacetic acid (NTA, see picture), a well-established practice in protein research, was used to improve the half-life of therapeutic proteins in the blood following systemic administration in vivo. Animal models show that this site-specific modification improves the efficacy of modified TRAIL proteins. As a service to our authors and readers, this journal provides support