Science Advances

Supplementary Materials

This PDF file includes:

  • Fig. S1. Acid stability of sialyloligosaccharide phenacyl ester.
  • Fig. S2. General scheme of the synthesis of a sialylglycopeptide-α-thioester by an improved Boc SPPS method.
  • Fig. S3. HPLC profile and ESI mass spectrum of H-Ala1-Gly28-α-thioester.
  • Fig. S4. HPLC profile and ESI mass spectrum of H-Cys29,33 (Acm)-Tyr49-α-thioester.
  • Fig. S5. HPLC profile and ESI mass spectrum of H-Cys(Acm)-Asn38(glycan)-Tyr49-α-thioester.
  • Fig. S6. HPLC profile and ESI mass spectrum of H-Cys79(Thz)-Trp88-(formyl)-Lys97-α-thioester.
  • Fig. S7. HPLC profile and ESI mass spectrum of H-Cys79(Thz)-Asn83(glycan)-Trp88(formyl)-Lys97-α-thioester.
  • Fig. S8. HPLC profile and ESI mass spectrum of H-Cys98(Thz)-Ala127-α-thioester.
  • Fig. S9. HPLC profile and ESI mass spectrum of H-Cys50-Ala78-α-hydrazide.
  • Fig. S10. HPLC profile and ESI mass spectrum of H-Ala1-Asn24(glycan)-Gly28-α-thioester.
  • Fig. S11. Monitoring NCL between H-Cys (Acm)-Asn38(glycan)-Tyr49-α-thioester and H-Cys50-Ala78-α-hydrazine.
  • Fig. S12. Monitoring NCL between H-Cys (Acm)-Asn38(glycan)-Ala78-α-hydrazide and H-Cys79-Asn83(glycan)-Arg166-OH.
  • Fig. S13. Monitoring the desulfurization reaction of H-Cys (Acm)-Cys -Asn (glycan)-Arg166-OH.
  • Fig. S14. Monitoring of the removal of Acm group of H-Cys (Acm)-Asn (glycan)2-Arg166-OH by RP-HPLC and ESI-MS.
  • Fig. S15. Monitoring the NCL between H-Ala1-Asn24(glycan)-Gly28-α-thioester and H-Cys29-Asn (glycan)2-Arg166-OH.
  • Fig. S16. The folding reaction of EPON24, N38, N83 (polypeptide form of H-Ala1-Asn (glycan)3-Arg166-OH.
  • Fig. S17. The folding reactions of EPON38, N83 (polypeptide form of H-Ala1-Asn (glycan)2-Arg166-OH) and EPON24, N83 (polypeptide form of H-Ala1-Asn24, 83(glycan)2-Arg166-OH).
  • Fig. S18. The folding reactions of EPON24, N38 (polypeptide form of H-Ala1-Asn (glycan)2-Arg166-OH) and EPON83 (polypeptide form of H-Ala1-Asn83(glycan)-Arg166-OH).
  • Results of folding experiments
  • Fig. S19. Monitoring of in vitro folding by SDS-PAGE.
  • Fig. S20. Analysis of disulfide bond positions of EPON24, N38, N83 2 by trypsin digestion.
  • Fig. S21. Analysis of disulfide bond positions of EPON38, N83 3 by trypsin digestion.
  • Fig. S22. Analysis of disulfide bond positions of EPON24, N83 by trypsin digestion.
  • Fig. S23. Analysis of disulfide bond positions of EPON24, N38 5 by trypsin digestion.
  • Fig. S24. Analysis of disulfide bond positions of EPON83 6 by trypsin digestion.
  • Fig. S25. Characterization of misfolded EPON24, N83 (compound 7).
  • High-resolution mass spectra of EPO glycoforms
  • Fig. S26. High-resolution mass spectrum of EPON24, N38, N83 2.
  • Fig. S27. High-resolution mass spectrum of EPON38, N83 3.
  • Fig. S28. High-resolution mass spectrum of EPON24, N38, 4.
  • Fig. S29. High-resolution mass spectrum of EPON38, N83 5.
  • Fig. S30. High-resolution mass spectrum of EPON83 6.

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