Cobalt(III)-induced hexamerization of PEGylated insulin

Lim, Sung In; Jang, Myung Hyun; Kim, Dae‐Jin; Bae, Sung Min; Kwon, Soyoung

doi:10.1016/j.ijbiomac.2011.07.019

Cited by 2 publications

(1 citation statement)

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“…Water soluble polyethylene glycols (PEGs) have been extensively employed to chemically modify the surface of protein macromolecules to inhibit their enzymatic breakdown and clearance by the kidneys. PEG binds to some specific surface areas of protein and prevents its hydrolysis without generating significant adverse effects ( 6 ). Synthesis of protein-polymer conjugates (so-called PEGylation process) exhibits a unique combination of properties derived from both biological and synthetic materials, which can be tailored to achieve the desired effect ( 7 ).…”

Section: Introductionmentioning

confidence: 99%

Application of SPRA Technology for Delivery of Erythropoietin: Stability Evaluation of Conjugated Erythropoietin with Adamantane and in SPRA Inclusion Complex

et al. 2023

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Background: As a widely used therapeutic protein, recombinant human erythropoietin (rhEPO) is currently one of the most effective biopharmaceuticals on the market for the treatment of anemia in patients with chronic renal disease. Increasing in vivo rhEPO’s half-life and its bioactivity is a significant challenge. It was hypothesized that the application of self-assembly PEGylation retaining activity, named supramolecular (SPRA) technology, could prolong the protein’s half-life without a significant loss of bioactivity. Objectives: This study aimed to assess the stability of rhEPO during synthetic reactions, including the conjugation with adamantane and the formation of the SPRA complex. To do this, the secondary structure of the protein was also evaluated. Methods: FTIR, ATR-FTIR, Far-UV-CD, and SDS-PAGE methods were employed. Thermal stability studies of the SPRA-rhEPO complex and rhEPO were investigated at 37°C for ten days using a nanodrop spectrophotometer. Results: The secondary structure of lyophilized rhEPO, AD-rhEPO, and rhEPO (pH 8) was compared to rhEPO. Results showed that the secondary structure of the protein was unaffected by lyophilization, pH change, and the formation of covalent bonds in conjugation reaction. SPRA-rhEPO complex was also stable for seven days in phosphate buffer (pH 7.4) at 37°C. Conclusions: It was concluded that the stability of rhEPO could increase by complexation using SPRA technology.

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Section: Introductionmentioning

confidence: 99%