Microbial transglutaminase-mediated formation of erythropoietin-polyester conjugates

Synthesis and Characterization of Dimeric Artesunate Glycerol Monocaprylate Conjugate and Formulation of Nanoemulsion Preconcentrate

“…Dimeric artesunate glycerol monocaprylate conjugate (D-AS-GC) was synthesized via a simple one-step Steglich esterification reaction [ 50 , 51 ]. Briefly, 0.5 g (2.29 mmol) of glycerol monocaprylate (GC) was dissolved in 40 mL of ice-cooled anhydrous DCM in a 100 mL 3-neck round-bottom flask equipped with a magnetic stirrer.…”

Enzymatic HES Conjugation with Recombinant Human Erythropoietin via Variant Microbial Transglutaminase TG16

“…T m of rHuEPO was determined as 54.3°C by nano-differential scanning fluorimetry (nanoDSF). [36] In order to expand the application of this enzymatic method, we further tested the reactivity of rHuEPO toward TG 16 using HES-g-NH 2 . It should be noted that the conjugation reaction of N-deglygosylated rHuEPO with the well-known fluorescent substrate of mTGase, MDC, was carried out at 37°C using mTGase-S2P and the SDS-PAGE results (see Figure S1 in the Supporting Information) show that no conjugation reaction took place at 37°C since the acceptance of rHuEPO as a substrate requires partial unfolding of the 3Dstructure.…”

“…[35] Recently, our group has reported a successful conjugation of rHuEPO with a sugar-based aminegrafted poly(D-sorbitol adipate) at the level of Gln residues using a highly thermoresistant variant of mTGase, TG 16 , at the transition temperature T m of rHuEPO (54.3°C). [36] Herein, we investigated the mTGase-catalyzed conjugation of recombinant human erythropoietin (rHuEPO) with aminemodified HES (HES-g-NH 2 ) to obtain an enzymatically synthesized carrier for rHuEPO delivery. Initially, we describe the synthesis of HES-g-NH 2 to obtain a potential substrate for mT-Gase by a one-step reaction of HES with hexamethylenediamine (HMDA) in the presence of 1,1′-carbonyldiimidazole (CDI).…”

“…[ 35 ] Recently, our group has reported a successful conjugation of rHuEPO with a sugar‐based amine‐grafted poly(D‐sorbitol adipate) at the level of Gln residues using a highly thermoresistant variant of mTGase, TG 16 , at the transition temperature T m of rHuEPO (54.3°C). [ 36 ]…”

Transglutaminase in Foods and Biotechnology

“…The main differences between microbial TGM and existing TGMs from animal sources are presented in Table 2. TGM-catalyzed reactions result in functional property changes, such as solubility foaming, viscosity, elasticity, water holding capacity, emulsifying capacity, gelation, and thermal stability of different food proteins [23][24][25]. TGM was also found to be involved in many physiological processes, such as in coagulation antibacterial immune reactions and in photosynthesis.…”