saporin

Wang J, Zhang S, Li Y, Xu Q, Kritzer JA (2024) Investigating the cytosolic delivery of proteins by lipid nanoparticles using the chloroalkane penetration assay. Biochemistry doi: 10.1021/acs.biochem.3c00614 PMID: 38334719

Objective: To investigate bovine serum albumin (BSA) protein encapsulation and release within polylysine/polyglutamate (PLys/PGlu) coacervates.

Summary: The findings emphasize the importance of ingredient addition sequence in coacervate formation and encapsulation rates, attributed to preference contact between oppositely charged proteins and poly(amino acid)s.

Usage: The positively-charged saporin and lysozyme protein exhibited the highest encapsulation efficiency when first combined with PGlu, followed by the addition of PLys in simulations of the coacervate encapsulation of saporin.

Related Products: Saporin (Cat. #PR-01)

Lv X, Martin J, Hoover H, Joshi B, Wilkens M, Ullisch DA, Leibold T, Juchum JS, Revadkar S, Kalinovska B, Keith J, Truby A, Liu G, Sun E, Haserick J, DeGnore J, Conolly J, Hill AVS, Baldoni J, Kensil C, Levey D, Spencer AJ, Gorr G, Findeis M, Tanne A (2024) Chemical and biological characterization of vaccine adjuvant QS-21 produced via plant cell culture. iScience 27(3):109006. doi: 10.1016/j.isci.2024.109006 PMID: 38361610

Objective: To report for the first time successful plant cell culture production of Quillaja saponaria (QS)-21 having structural, chemical, and biological properties similar to the bark-extracted product.

Summary: The data demonstrate that cell culture is a sustainable alternative to natural resources to produce QS-21 as an adjuvant. In this proof-of-concept approach, it’s shown that the chemical, biochemical, and biophysical equivalence of bark extract and cell culture-derived QS-21 translate into conserved biological and adjuvant properties both in vitro and in vivo.

Usage: Pseudo cross-presentation assays (25 ng/mL Saporin).

Related Products: Saporin (Cat. #PR-01)

Lu S, Gan L, Lu T, Zhang K, Zhang J, Wu X, Han D, Xu C, Liu S, Yang F, Qin W, Wen W (2024) Endosialin in cancer: Expression patterns, mechanistic insights, and therapeutic approaches. Theranostics 14(1):379-391. doi: 10.7150/thno.89495 PMID: 38164138

Objective: To discuss the use of a saporin conjugate to 78Fc, an antibody fragment directed towards endosialin a.k.a. CD248, in the treatment of human sarcomas.

Summary: Endosialin/CD248 is over expressed in cancer and a human single-chain variable fragment -Fc fusion protein was created targeting this receptor, 78Fc. 78Fc was then conjugated to saporin creating an immunotoxin. 78Fc-SAP is discussed as a immunotoxic strategy for the treatment of endosialin-based treatment therapies in cancer.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Guo Y et al. Tumour endothelial marker 1/endosialin-mediated targeting of human sarcoma. Eur J Cancer 90:111-121, 2018.

Gong S, Qiu J, Thayumanavan S (2024) Self-assembly of epitope-tagged proteins and antibodies for delivering biologics to antigen presenting cells. J Am Chem Soc 146(1):33-38. doi: 10.1021/jacs.3c09334 PMID: 38147631

Objective: To describe a simple self-assembly strategy for generating artificial immune complexes.

Summary: The built-in recognition domains in the antibody, viz. the Fab and Fc domains, are judiciously leveraged for cargo conjugation to generate the nanoassembly and macrophage targeting, respectively. A responsive linker is engineered into the nanoassembly for releasing the protein cargo inside the macrophages while ensuring stability during delivery.

Usage: Cytotoxicity assay to measure cell death with targeted saporin.

Related Products: Saporin (Cat. #PR-01)

Bortolotti M, Biscotti F, Zanello A, Polito L, Bolognesi A (2024) Heterophyllin: A new adenia toxic lectin with peculiar biological properties. Toxins 16(1):1. doi: 10.3390/toxins16010001 PMID: 38276525

Objective: Describe the novel type II Ribosome Inactivating Protein, Heterophyllin.

Summary: Heterophyllin, a novel toxic lectin from Adenia heterophylla shows enzymatic and lectin properties of type 2 RIPs. Heterophyllin was able to completely abolish cell viability at nM concentration. The enzymatic, immunological, and biological activities of heterophyllin provide interest in possible pharmacological application.

Usage: Saporin is used as a Type I Ribosome Inactivating Protein to compare it to Heterophyllin, a type II RIP.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Bortolotti, M.; Biscotti, F.; Zanello, A.; Bolognesi, A.; Polito, L. New insights on saporin resistance to chemical derivatization with heterobifunctional reagents. Biomedicines 2023, 11, 1214.

Chan A, Tsourkas A (2024) Intracellular protein delivery: Approaches, challenges, and clinical applications. BME Frontiers 5:0035. doi: 10.34133/bmef.0035 PMID: 38282957

Objective: To review progress made towards achieving cytosolic delivery of recombinant proteins and possible strategies to enable proteins to cross cell membranes.

Summary: Drug delivery researchers have worked to deliver saporin into tumor cells in the hopes of producing potent next-generation cancer therapeutics. Cationic, anionic, and zwitterionic versions of poly(β-amino ester) have been developed for delivery of saporin. Chemically-modified saporin can be encapsulated by cationic LNPs for in vivo tumor inhibition. Saporin has been used as a model cargo protein for in vivo delivery via fluoropolymer nanoparticles for successful tumor growth inhibition.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Ancheta LR et al. Saporin as a commercial reagent: its uses and unexpected impacts in the biological sciences-tools from the plant kingdom. Toxins (Basel) 14(3):184, 2022.

di Leandro L, Colasante M, Pitari G, Ippoliti R (2023) Hosts and heterologous expression strategies of recombinant toxins for therapeutic purposes. Toxins (Basel) 15(12):699. doi: 10.3390/toxins15120699 PMID: 38133203

Objective: Review the recombinant expression of toxins from bacterial, plant, or animal species used as components of immunotoxins.

Summary: Commercial production of recombinant proteins for therapeutic purposes involves the utilization of various hosts, with the most common choices being bacteria, yeasts, and mammalian cell lines. The authors also provide an overview of the primary advantages and disadvantages of various systems for toxin manufacturing.

Related Products: Saporin (Cat. #PR-01)

Singh RR, Mondal I, Janjua T, Popat A, Kulshreshtha R (2023) Engineered smart materials for RNA based molecular therapy to treat Glioblastoma. Bioact Mater 33:396-426. doi: 10.1016/j.bioactmat.2023.11.007 PMID: 38059120

Objective: A review of non-coding RNA therapy and its targeted delivery of nucleic acids to treat Glioblastoma, emphasizing smart nano-materials.

Summary: Nano-carriers of ncRNA can offer unique advantages in fighting, such as low cytotoxicity, ability to cross the blood-brain barrier, stealth to bypass immune detection, prolonged release of the cargo, improved circulatory time, and also targeted therapy.

Usage: Saporin as a payload to the nano-carriers angiopep-2 peptide and RAP12.

Related Products: Saporin (Cat. #PR-01)

Chamberlain AR, Huynh L, Huang W, Taylor DJ, Harris ME (2023) The specificity landscape of bacterial ribonuclease P. J Biol Chem 300(1):105498. doi: 10.1016/j.jbc.2023.105498 PMID: 38013087

Objective: Review of the specificity of ribonucleoprotein RNase P in binding different types of RNA.

Summary: Ribonucelase P is involved in the RNA metabolism pathways. By studying the rate at which it combines with different types of RNA under different conditions, like concentration and competition with different enzymes, a model describing its specificity to different RNA motifs can be developed.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Hauf, S., Rotrattanadumrong, R., and Yokobayashi, Y. (2022) Analysis of the sequence preference of saporin by deep sequencing. ACS Chem. Biol.17, 2619–2630

Makarova AO, Kostenk VV, Ovsyanikova OV, Svirshchevskaya EV, Lutsenko GV, Lutsenko AM (2023) Heat shock proteins on tumor cell surface as target for anti-tumor therapy (a review). Russian Journal of Bioorganic Chemistry 50(3):644-656. doi: 10.1134/S1068162024030038

Objective: To present the characteristics of the main proteins of the heat shock proteins (HSP) family, the features of their expression in tumor cells, and the possibility of using monoclonal antibodies against these proteins as a guiding vector for anti-tumor immunotherapy.

Summary: Apart from targeted delivery of NPs and different therapeutic drugs into cancer cells, another advantage of mAbs against HSP70 is their ability to activate anti-tumor antibody-dependent cellular cytotoxicity.

Usage: Certain antitumor drugs can be delivered by mAbs not only as part of NPs, but also as a drug–antibody conjugate. For instance, anti-HSP65 mouse mAb ML30 conjugated to Saporin (PR-01) almost fully inhibited cell proliferation of cell lines U937 and Daudi that express HSP65 on their surfaces.

Related Products: Saporin (Cat. #PR-01), Custom Conjugates