This golden autumn, SINOPEG ventured to Europe with its innovative products and solutions, making consecutive appearances at two premier international industry exhibitions within two months, engaging in deep exchanges with global pharmaceutical elites. CPHI Frankfurt 2025 (Frankfurt, Germany, Oct 28-30) As the world's largest and most influential professional event for the pharmaceutical industry, CPHI Frankfurt brought together industry elites from across the globe. In this grand gathering, SINOPEG attracted numerous visitors with its professional technical sharing. During the exhibition, we prominently showcased our latest achievements in areas such as in vivo CAR-T delivery, Antibody-Drug Conjugate (ADC) linkers, and block copolymers. We held in-depth discussions with multiple potential clients and partners from Europe, North America, and Asia! Many international clients praised our continuously improving R&D capabilities and product quality control system. TIDES Europe 2025 (Basel, Switzerland, Nov 11-13) Following closely, we moved to Switzerland to participate in TIDES Europe, an exhibition focused on oligonucleotides, peptides, mRNA therapies, and related fields. As one of the fastest-growing segments in biopharmaceuticals, TIDES provided us with a valuable platform for direct dialogue with global top experts. Here, we shared SINOPEG's technical expertise and project experience in fatty acid-modified side chains, LNP delivery material production, and related CMC services, attracting numerous biotechnology companies seeking reliable CDMO partners in this field. Through exchanges with industry benchmark companies, we further clarified our future technological development direction and innovation priorities. The successful participation in these two consecutive exhibitions allowed us to clearly grasp the development pulse of the global pharmaceutical industry chain. We deeply felt that CDMO enterprises from China are increasingly winning the trust of the global market, thanks to their continuously enhancing technical capabilities, flexible service models, and reliable quality systems. Two expeditions, two stages of growth. We brought back customer recognition, partner trust, and market insights – all of which will be invaluable assets for SINOPEG's future development! SINOPEG's journey on the international stage has just begun. We will continue to deepen our core technologies and expand our global footprint. Next year, we will appear on broader international stages, bringing more innovative solutions 'Made in China' to the global pharmaceutical industry. Stay tuned!

Join Us at TIDES Europe 2025 in Congress Center Basel! Mark your calendars!TIDES Europe2025—the premier event for oligonucleotide and peptide therapeutics—is coming to Basel, Switzerland, on 11-13 November 2025. Visit SINOPEG at Booth #333 to explore cutting-edge solutions in: Custom PEG Derivatives (mPEG, heterobifunctional PEGs, branched PEGs) Lipid Nanoparticles (LNPs) & Lipidoids for nucleic acid delivery Innovative Linker Technologies & ADC Payloads Why Stop By? Discuss your formulation challenges with our PEGylation experts Discover high-purity excipients for mRNA, siRNA, and peptide therapies Learn how our GMP-grade materials accelerate preclinical-to-commercial transitions Spotlight Case Study: Ask us about our role in developing temperature-stable LNP formulations for a global COVID-19 vaccine partner! Schedule a 1:1 Meeting: Avoid the crowds—reserve your private session today: sales@sinopeg.com Can't attend? Explore our solutions online: http://www.sinopeg.com Let's shape the future of oligonucleotide and peptide therapeutics together! See you at #333. #TIDES2025 DrugDiscovery #LNPs #mRNA #PeptideTherapeutics #BiotechInnovation

Molecules. 2017 Jul 15;22(7):1190. doi: 10.3390/molecules22071190. Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length Abstract A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals. Keywords: antiviral; cholesterol; membranes; paramyxoviruses; peptides. PEG Linker: Various Kingds And Grades Of Such Monodispersed Are Readily Avaliable| SINOPEG

Join Us at 2025 CPHI Worldwide Europe! SINOPEG's booth no. 8.0T48 Exciting news! 2025 CPHI Worldwide Europe is just around the corner, taking place October 28–30 at Messe Frankfurt. SINOPEG will be showcasing cutting-edge drug delivery system (DDS) solutions at Booth 8.0T48.    As your trusted partner in specialty chemicals and advanced drug delivery systems, we’re eager to share innovations that drive industry progress. Why visit us? Explore our latest portfolio of PEG derivatives, lipids, and custom synthesis services Discuss tailored solutions for your R&D and manufacturing challenges Connect face-to-face with our technical experts We warmly welcome friends, partners, and industry peers from around the globe to drop by!    Let’s collaborate to shape the future of pharma. Dates: October 28–30, 2025 Venue: Messe Frankfurt Our Booth: T48 (Hall 8.0) Ready to meet? Simply stop by!

Join Us at CPhI Worldwide 2025–The Premier Global Pharma Event!   We are excited to invite you to visitSINOPEG at CPhI Worldwide 2025, the world‘s leading pharmaceutical industry gathering. This premier event brings together industry leaders, innovators, and experts from across the entire pharmaceutical supply chain—including APIs, formulations, biopharma, and outsourcing services.   Event Details: Date: October 28–30, 2025 Location: Frankfurt, Germany Booth: 8.0T48   At Booth 8.0T48, we will showcase our comprehensive technical capabilities and global service solutions tailored to meet the evolving needs of the pharmaceutical industry. This is a great opportunity to explore how SINOPEG can support your business with innovation, quality, and reliability.   We look forward to connecting with you, discussing potential collaborations, and sharing insights into the future of pharma.   Save the date and stop by—we can’t wait to welcome you!   Warm regards, The SINOPEG Team

J Pharm Sci. 2020 Feb;109(2):981-991.  doi: 10.1016/j.xphs.2019.10.052.  Epub 2019 Nov 2. Conjugation of Amine-Functionalized Polyesters With Dimethylcasein Using Microbial Transglutaminase Abstract Protein-polymer conjugates have been used as therapeutics because they exhibit frequently higher stability, prolonged in vivo half-life, and lower immunogenicity compared with native proteins.  The first part of this report describes the enzymatic synthesis of poly(glycerol adipate) (PGA(M)) by transesterification between glycerol and dimethyl adipate using lipase B from Candida antarctica.  PGA(M) is a hydrophilic, biodegradable but water insoluble polyester.  By acylation, PGA(M) is modified with 6-(Fmoc-amino)hexanoic acid and with hydrophilic poly(ethylene glycol) side chains (mPEG12) rendering the polymer highly water soluble.  This is followed by the removal of protecting groups, fluorenylmethyloxycarbonyl, to generate polyester with primary amine groups, namely PGA(M)-g-NH2-g-mPEG12.  1H NMR spectroscopy, FTIR spectroscopy, and gel permeation chromatography have been used to determine the chemical structure and polydispersity index of PGA(M) before and after modification.  In the second part, we discuss the microbial transglutaminase-mediated conjugation of the model protein dimethylcasein with PGA(M)-g-NH2-g-mPEG12 under mild reaction conditions.  SDS-PAGE proves the protein-polyester conjugation. Keywords: CAL-B;  amine-functionalized polyester;  enzymatic polymerization;  microbial transglutaminase (mTGase);  poly(glycerol adipate) (M);  protein-polymer conjugate.

Bioconjug Chem. 2025 Feb 19;36(2):179-189.  doi: 10.1021/acs.bioconjchem.4c00392.  Epub 2025 Jan 20. PEGylation of Dipeptide Linker Improves Therapeutic Index and Pharmacokinetics of Antibody-Drug Conjugates Abstract Hydrophobic payloads incorporated into antibody-drug conjugates (ADCs) typically are superior to hydrophilic ones in tumor penetration and "bystander killing" upon release from ADCs.  However, they are prone to aggregation and accelerated plasma clearance, which lead to reduced efficacies and increased toxicities of ADC molecules.  Shielding the hydrophobicity of payloads by incorporating polyethylene glycol (PEG) elements or sugar groups into the ADC linkers has emerged as a viable alternative to directly adopting hydrophilic payloads.  In this study, ADC linkers incorporating PEG or sugar groups were synthesized by modifying dipeptide linkers, with hydrophobic monomethyl auristatin E (MMAE) serving as an exemplary hydrophobic payload.  All drug-linkers (DLs) were conjugated to RS7, a humanized antibody targeting Trop-2, with drug-to-antibody ratio (DAR) values set at 4 or 8.  Among these, the ADC molecule RS7-DL 11, featuring a methyl-PEG24 (mPEG24) moiety as a side chain to the Valine-Lysine-PAB (VK) linker, demonstrated maximum hydrophilicity, biophysical stability, and tumor suppression, along with prolonged half-life and enhanced animal tolerability.  In conclusion, through PEGylation of the traditional dipeptide linker, we have demonstrated an optimized ADC conjugation technology that can be employed for conjugating ultrahydrophobic payloads, thus enhancing both the therapeutic index and pharmacokinetics profile.

Langmuir. 2014 Jul 1;30(25):7465-74. doi: 10.1021/la500403v. Epub 2014 Jun 17. Effect of polyethylene glycol, alkyl, and oligonucleotide spacers on the binding, secondary structure, and self-assembly of fractalkine binding FKN-S2 aptamer-amphiphiles Abstract Previously we identified an aptamer, named FKN-S2, which binds the cell surface protein fractalkine with high affinity and specificity. In this paper a hydrophobic dialkyl C16 tail was added to the aptamer to create an aptamer-amphiphile. We investigated how the tail and a spacer molecule of varying length and hydrophobicity, inserted between the tail and the aptamer headgroup, affect the binding, structure, and self-assembly properties of the aptamer-amphiphile. We synthesized aptamer-amphiphiles with no spacer (NoSPR), polyethylene glycol (PEG4, PEG8, PEG24), alkyl (C12 and C24), or oligonucleotide (T10 and T5: 10 and 5 thymine, and A10: 10 adenine) spacers. The addition of the tail reduced the binding affinity of the aptamer-amphiphile over 7.5-fold compared to the free aptamer. The hydrophobic alkyl spacers resulted in the greatest loss of affinity, and the hydrophilic PEG spacers improved amphiphile affinity but did not restore it to that of the free aptamer. Interestingly, oligonucleotide spacers produced the highest affinity amphiphiles. Nucleotide composition did not affect affinity, however, as the T10 and A10 spacers had equal affinity. The oligonucleotide spacer amphiphiles had the highest affinity because the oligonucleotide spacer increased the affinity of free aptamer; the FKN-S2 aptamer plus the oligonucleotide spacer had a higher affinity than the free FKN-S2 aptamer. Circular dichroism (CD) spectroscopy and thermal melting studies indicated the aptamer forms a stem-loop and intramolecular G-quadruplex, and the tail strongly stabilized the formation of the G-quadruplex in a buffer. Cryogenic transmission electron microscopy (cryo-TEM) imaging showed the aptamer-amphiphiles, independent of the spacer used, self-assembled into micelles and nanotapes, flat bilayer structures that were often twisted. Finally, liposomes functionalized with the FKN-S2 amphiphile were incubated with fractalkine expressing cells, and the amount of binding was dependent on the concentration of the amphiphile on the liposome surface.