Id |
Subject |
Object |
Predicate |
Lexical cue |
T46 |
0-2 |
Sentence |
denotes |
2. |
T47 |
3-10 |
Sentence |
denotes |
Results |
T48 |
12-16 |
Sentence |
denotes |
2.1. |
T49 |
17-66 |
Sentence |
denotes |
Cloning and Bacterial Production of PASylated Tα1 |
T50 |
67-460 |
Sentence |
denotes |
To achieve C-terminal PASylation of N-terminally acetylated Tα1, a plasmid harboring a bicistronic operon was constructed to allow the simultaneous expression of human Tα1 (UniProtKB ID: P06454; residues 2–29), C-terminally fused with a PAS polypeptide comprising 601 amino acids [34], and the E. coli N-acetyltransferase RimJ (UniProtKB ID: P0A948) based on the vector pASK75 (Figure 1) [36]. |
T51 |
461-643 |
Sentence |
denotes |
In a parallel attempt, a plasmid encoding an N-terminally PASylated Tα1 was constructed, again, using plasmid pASK75 as the backbone (this time omitting the RimJ cistron, see below). |
T52 |
644-832 |
Sentence |
denotes |
Cytoplasmic gene expression was performed in both cases on a 2 L shake flask scale using the E. coli strain NEBexpress under control of the chemically inducible tet promoter/operator [36]. |
T53 |
833-922 |
Sentence |
denotes |
The whole cell lysate was analyzed prior to and 15 h after induction by Western blotting. |
T54 |
923-1228 |
Sentence |
denotes |
Using a monoclonal antibody that recognizes an epitope of the PAS#1 sequence, a distinct band with an approximate molecular size above 250 kDa was detected (Figure 1b), which demonstrated successful bacterial expression of the full-length C-terminally PASylated Tα1 (Tα1-PAS) without signs of degradation. |
T55 |
1229-1545 |
Sentence |
denotes |
Of note, the unusually slow migration of Tα1-PAS (52.7 kD) in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) is well known for PASylated proteins [31,37] and can be explained by the poor binding of SDS (which provides the electrophoretic driving force) to the strongly hydrophilic PAS sequence. |
T56 |
1547-1551 |
Sentence |
denotes |
2.2. |
T57 |
1552-1611 |
Sentence |
denotes |
Purification and In Vitro Characterization of PASylated Tα1 |
T58 |
1612-1831 |
Sentence |
denotes |
The uncharged PAS moiety, which does not alter the isoelectric point of the target peptide, facilitates classical protein precipitation by ammonium sulfate, thus providing an efficient and inexpensive purification step. |
T59 |
1832-2076 |
Sentence |
denotes |
After adjusting the cleared whole cell extract prepared by mechanical cell lysis to 30% ammonium sulfate saturation, most of the host cell proteins remained in solution while both PAS-Tα1 and PAS-Tα1 were selectively recovered as a precipitate. |
T60 |
2077-2243 |
Sentence |
denotes |
To remove residual E. coli proteins, the redissolved precipitate was subjected to ion exchange chromatography on a salt-tolerant anion exchange (AEX) resin at pH 8.5. |
T61 |
2244-2511 |
Sentence |
denotes |
Even though the PASylated Tα1 peptide with a calculated pI of 4.3 [38] for both versions should be negatively charged under these conditions and, hence, is expected to adsorb to the resin, the recombinant fusion proteins were quantitatively found in the flow-through. |
T62 |
2512-2640 |
Sentence |
denotes |
Possibly, the voluminous PAS polymer partially shields the small peptide from ionic interactions with the chromatography matrix. |
T63 |
2641-2761 |
Sentence |
denotes |
Nevertheless, this step resulted in efficient depletion both of residual host cell proteins and of bacterial endotoxins. |
T64 |
2762-3043 |
Sentence |
denotes |
The protein solutions were dialyzed against a citrate buffer at pH 3.0 and subsequently applied to a strong cation exchange (CEX) column, which resulted in a bound fraction for PAS-Tα1, whereas both a flow-through fraction and a bound fraction were observed for Tα1-PAS (Figure 2). |
T65 |
3044-3292 |
Sentence |
denotes |
Electrospray ionization mass spectrometry (ESI-MS) analysis of Tα1-PAS in the flow-through revealed a molecular mass of 52,734.56 Da (Figure 2a), which exactly matches the calculated mass for the N-terminally acetylated gene product (52,734.56 Da). |
T66 |
3293-3497 |
Sentence |
denotes |
In this case, the start methionine of Tα1-PAS (followed by a Ser residue) was fully processed, presumably by the bacterial methionine aminopeptidase [39], then followed by N-terminal acetylation via RimJ. |
T67 |
3498-3849 |
Sentence |
denotes |
In contrast, the column-bound peptide fraction, which was eluted using a salt concentration gradient, showed a molecular mass of 52,692.38 Da (Figure 2b), which corresponds to the calculated mass for the non-acetylated processed polypeptide (52,692.54 Da) accompanied by some minor peaks below 40 kDa, most likely due to residual host cell impurities. |
T68 |
3850-4008 |
Sentence |
denotes |
Accordingly, this CEX step enabled separation of the desired N-acetylated Tα1-PAS from its non-acetylated precursor as a result of a single charge difference. |
T69 |
4009-4200 |
Sentence |
denotes |
In comparison, the fully column-bound non-acetylated PAS-Tα1 showed a single molecular mass of 52,789.8 Da (Figure 3) corresponding to the intact peptide, again, lacking the start methionine. |
T70 |
4201-4327 |
Sentence |
denotes |
Both PASylated peptide preparations had a purity > 96% as indicated by reverse-phase chromatography (Figure 2c and Figure 3c). |
T71 |
4328-4430 |
Sentence |
denotes |
For Tα1-PAS, we performed a final AEX polishing step, which also allowed concentration of the peptide. |
T72 |
4431-4557 |
Sentence |
denotes |
At pH 10, the acetylated Tα1-PAS bound to a strong AEX resin and eluted as a homogenous peak in a salt concentration gradient. |
T73 |
4558-4704 |
Sentence |
denotes |
The endotoxin content of this fraction was very low, with < 0.1 EU/mg, and the final yield was 15 mg acetylated Tα1-PAS per 1 L bacterial culture. |
T74 |
4705-4906 |
Sentence |
denotes |
In comparison, the final yield of the fully column-bound (non-acetylated) PAS-Tα1 reached 50 mg per 1 L bacterial culture after CEX chromatography and, again, the endotoxin content was below 0.1 EU/mg. |
T75 |
4907-5095 |
Sentence |
denotes |
Analytical size exclusion chromatography (SEC) of both PASylated peptide versions revealed a single symmetric peak without any signs of aggregation or truncation (Figure 2d and Figure 3d). |
T76 |
5096-5162 |
Sentence |
denotes |
The N-terminally acetylated Tα1-PAS eluted at 13.5 mL (bed volume: |
T77 |
5163-5284 |
Sentence |
denotes |
24 mL), whereas PAS-Tα1 eluted at 13.2 mL, thus indicating apparent molecular sizes of 557 kDa and 665 kDa, respectively. |
T78 |
5285-5595 |
Sentence |
denotes |
This is more than 10 times (Tα1-PAS) or even 12 times (PAS-Tα1) larger than the true molecular mass of both PASylated peptides (52.7 kDa), which demonstrates the huge expansion of the hydrodynamic molecular volume caused by the random-coil structure of the PAS polymer, in line with previous observations [35]. |
T79 |
5597-5601 |
Sentence |
denotes |
2.3. |
T80 |
5602-5659 |
Sentence |
denotes |
PASylation Strongly Prolongs Tα1 Pharmacokinetics in Rats |
T81 |
5660-5817 |
Sentence |
denotes |
To mimic the clinically approved route of Zadaxin™ administration, the N-acetylated Tα1-PAS was injected subcutaneously into the dorsal area of rats (N = 5). |
T82 |
5818-5954 |
Sentence |
denotes |
The injected dose of 3.4 mg/kg Tα1-PAS was well tolerated without any drug-related adverse events or significant changes in body weight. |
T83 |
5955-6176 |
Sentence |
denotes |
The Tα1-PAS plasma levels at various sampling times were analyzed using a quantitative sandwich ELISA developed to detect only Tα1-PAS and no endogenous rat Tα1, which shares 100% sequence identity with the human peptide. |
T84 |
6177-6352 |
Sentence |
denotes |
The pharmacokinetic (PK) profile of Tα1-PAS (Figure 4) exhibited a typical curve according to the Bateman function [40], with a Cmax of 25.6 ± 4.4 mg/L at tmax = 22.7 ± 1.1 h. |
T85 |
6353-6571 |
Sentence |
denotes |
Curve fitting with the WinNonlin software revealed a drastically extended terminal half-life of 15.9 ± 0.9 h, which is more than 8-fold longer than the one for the native peptide (τ1/2 = 1.9 h) published for rats [41]. |
T86 |
6572-6739 |
Sentence |
denotes |
The strong impact of PASylation on the PK profile is also reflected by other parameters such as the large area under the curve (AUC) and slow clearance (CL) (Table 1). |