• The Korean journal of internal medicine
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• 제33권6호
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• pp.1081-1083
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• 2018

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
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• pp.695-698
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• 2000

We studied the viability and function of islet with monomethoxy polyethylene glycol (mPEG) grafted onto its membrane. Islets were isolated from rat and were repeatedly reacted with activated mPEG (mw 5000) in order to increase grafting density. The density of grafted PEG on the islet membrane was confirmed by Fluorescein-PEG-NHS. An assessment of islet viability using AO / PI staining method showed that multiple PEGylation did not reduce islet viability. The function of PEG grafted islets was evaluated by measuring released insulin from islets. Insulin secreted from the PEGylated islets for 1 h did not show any significant difference compared to control (non-PEGylated) islets. In addition, PEGylated islets responded in the same pattern as control islets in the perifusion test.

• 한국표면공학회:학술대회논문집
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• 한국표면공학회 2012년도 추계총회 및 학술대회 논문집
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• pp.84-85
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• 2012

Poly(ethylene glycol) (PEG)는 Hydrophilic하면서 독성이 없기 때문에 약물과 관련된 연구가 많이 이루어졌다. 초기 PEGylation은 약물과 관련된 연구가 주를 이루었지만, 최근에는 PEG의 non-fouling 효과 때문에 표면에 적용하여 biomedical 장비에 세포나 단백질이 붙지 않도록 하는 개질하는 방법에 많은 연구가 진행되고 있다. Native Chemical Ligation(N.C.L.)은 단백질을 합성할 때, Protecting group을 사용하지 않고 반응을 진행시킬 수 있기 때문에 많은 주목을 받고 있다. N.C.L.은 합성한 두 물질이 Thioester와 Cysteine을 갖고 있으면, mild condition에서 amide bond를 형성하면서 반응이 쉽게 진행되기 때문에 다양한 분야에 적용할 수 있다. 이 논문에서 우리는 N.C.L.을 표면에 적용시켰으며 그 중 한 예로 표면 PEGylation진행하였다.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVI)
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• pp.375-375
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• 2005

• 대한약학회:학술대회논문집
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• 대한약학회 2000년도 NEW STRATEGY FOR DRUG DEVELOPMENT IN POST-GENOMIC ERA(대한약학회)
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• pp.269.2-270
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• 2000

• 대한약학회:학술대회논문집
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• 대한약학회 2000년도 춘계총회 및 학술대회
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• pp.199.2-199.2
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• 2000

• 대한방사성의약품학회지
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• 제6권2호
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• pp.155-164
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• 2020

Polyethylene glycol (PEG) has been the most commonly used polymer for the past few decades in the field of biomedical applications due to its gold standard stealth effect. PEGylation of antibody-drug conjugates, liposomes, peptides, nanoparticles, and proteins is done to improve their pharmaceutical efficacy and pharmacokinetic properties. PEGylation of antibodies with various PEG linkers improves targeting ability by increasing the blood circulation time and thus enhances the biodistribution profiles. It also assists in minimizing the immediate capture by the reticuloendothelial system. In this review, we summarize the effect of PEG linkers in an antibody conjugation and their pharmacokinetics in the field of biomedical imaging.

• Journal of Microbiology and Biotechnology
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• 제17권10호
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• pp.1670-1674
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• 2007

Duffy binding protein (DBP) plays a critical role in Plasmodium vivax invasion of human red blood cells. We previously reported a single-chain antibody fragment (scFv) that was specific to P. vivax DBP (PvDBP). However, the stabilization and the half-life of scFvs have not been studied. Here, we investigated the effect of PEGylated scFvs on their biological activity and stability in vitro. SDS-PAGE analysis showed that three clones (SFDBII-12, -58, and -92) were formed as monomers (about 70 kDa) with PEGylation. Clone SFDBII-58 gave the highest yield of PEGylated scFv. Binding analysis using BIAcore between DBP and scFv showed that both SFDBII-12 and -58 were decreased approximately by two folds at the level of binding affinity to DBP after PEGylation. However, the SFDBII-92 clone still showed a relatively high level of binding affinity ($K_D=1.02{\times}10^{-7}\;M$). Binding inhibition assay showed that PEGylated scFv was still able to competitively bind the PvDBP and playa critical role in inhibiting the interactions between PvDBP protein expressed on the surface of Cos-7 cells and Duffy receptor on the surface of erythrocytes. When both scFvs and their PEGylated counterparts were exposed to trypsin, scFv was completely degraded only after 24 h, whereas 35% of PEGylated scFvs remained intact, maintaining their stability against the proteolytic attack of trypsin until 72 h. Taken together, these results suggest that the PEGylated scFvs retain their stability against proteolytic enzymes in vivo, with no significant loss in their binding affinity to target antigen, DBP.

• 대한약학회:학술대회논문집
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• 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
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• pp.298.2-298.2
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• 2003

The insulinotropic hormone, glucagons-like peptide-1 (GLP-1), which has been proposed as a new potential therapeutics for type-II diabetes, but this is metabolized extremely rapidly by the ubiquitous enzyme, dipeptidyl peptidase IV (DPP IV), forming a metabolite, which acts as an antagonist at the GLP-1 receptor. (omitted)

• 대한약학회:학술대회논문집
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• 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
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• pp.220.2-220.2
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• 2002