Table 2. Comparison of PEGylation methods for L-asparaginase.
Modification specificitya | Modification degree (%)b | Activity (%)c | Reference |
---|---|---|---|
PEG Dichloro-s-triazine (5000 Da) | 20–79 | 45–11 | Ashihara et al. [16] |
1900 Da | 76 | 20 | Ashihara et al. [16] |
750 Da | 84 | 16 | Ashihara et al. [16] |
PEG Vinylpyrrolidone-maleic acid (5000 Da) | 33 | 59 | Qian et al. [17] |
PEG Succinimidyl succinate (5000 Da) | 54 | 30 | Soares et al. [18] |
PEG Propionaldehyde (20000 Da) | 4 | 44 | Wang et al. [19] |
PEG Chloro-s-triazine (10000 Da) | 57 | 11 | Matsushima et al. [20] |
PEG Chloro-s-triazine (10000 Da) | 57 | 8 | Kamisaki et al. [21] |
PEG Comb-shaped (100000 Da) | 34 | 86 | Kodera et al. [22] |
13000 Da | 50 | 46 | Kodera et al. [22] |
PEG Monosulfone (5000, 10000 & 20000 Da) | 4 | 100 | Balan et al. [34] |
Dextran-glutaraldehyde | 99 | 35 | Balcão et al. [58] |
Dimethylsuberimidate | 25 | 17 | Handschumacher & Gaumond [59] |
PEG Bi-maleimide (5000 Da) | 9 | 130 | This work |
aModification specificity refers to the functional group in the polymer that is conjugated to L-asparaginase.
bModification degree refers to the average percentage of conjugated sites in comparison to the total amine groups per L-asparaginase tetramer.
cActivity refers to the relative catalytic activity of the bio-PEG-conjugate compared to the non-conjugated L-asparaginase defined as 100% and as reported by each study.