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1. 21st century Latin American synthetic peptides for their application in antivenom production

Author

Jésica A. Rodríguez, Gabriela R. Barredo-Vacchelli, Joaquin A. Eloy, and Silvia A. Camperi

Subjects
snake, scorpion, spider, animal envenoming, epitope mapping, solid-phase peptide synthesis, immunization, Pharmacy and materia medica, RS1-441
Abstract

Envenomation caused by snakes, scorpions, and spiders represents a serious public health problem in Latin America. The antivenoms used for its treatment are produced by immunizing horses repeatedly with sublethal doses of animal venoms along with the adjuvant. However, venom availability is a bottleneck. Furthermore, toxin-neutralizing antibodies are only a few of the total produced with this classical method. Therefore, high doses of antivenom are required to achieve the neutralization power, which usually causes adverse reactions in the patient. With the aim of obtaining a higher proportion of toxin-neutralizing antibodies while reducing the dependency on venom availability, alternative immunization protocols have been explored using synthetic peptides with epitopes from clinically relevant toxins. The process to design an immunogenic peptide entitles: (a) choice of the medical relevant toxins in the venom; (b) identification of the epitopes in the selected toxins; (c) improvement of peptide immunogenicity; (d) immunogen synthesis; and e) in vitro and in vivo evaluation. The present article aims to review the advances in the design of immunogenic synthetic peptides for their application in antivenom production in Latin America during the 21st century. Epitopes have been identified from many clinically important toxins in Latin American snakes (snake venom metalloproteinases, snake venom serine proteases, crotamine, phospholipases A2, and three-finger toxins), scorpions (beta-mammal/insect toxin Ts1, alpha-mammal toxin Ts2, alpha-mammal toxin Ts3, toxin Ts4, and beta-mammal Tt1g neurotoxin), and spiders (dermonecrotic toxin and delta-ctenitoxin-Pn2a). Nevertheless, their application is still experimental, even though they are ideal for large-scale and low-cost antivenom production, factors that are necessary to meet national and regional demands.

Published
2024
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3. Synthetic peptides to produce antivenoms against the Cys-rich toxins of arachnids

Author

Silvia A. Camperi, Gerardo Acosta, Gabriela R. Barredo, Lucía C. Iglesias-García, Cleópatra Alves da Silva Caldeira, María C. Martínez-Ceron, Silvana L. Giudicessi, Osvaldo Cascone, and Fernando Albericio

Subjects
Scorpion, Spider, Venom, Epitope, Solid-phase peptide synthesis, Knottins, Toxicology. Poisons, RA1190-1270
Abstract

Scorpion and spider envenomation is treated with the appropriate antivenoms, prepared as described by Césaire Auguste Phisalix and Albert Calmette in 1894. Such treatment requires the acquisition and manipulation of arachnid venoms, both very complicated procedures.Most of the toxins in the venoms of spiders and scorpions are extremely stable cysteine-rich peptide neurotoxins. Many strategies have been developed to obtain synthetic immunogens to facilitate the production of antivenoms against these toxins. For example, whole peptide toxins can be synthesized by solid-phase peptide synthesis (SPPS). Also, epitopes of the toxins can be identified and after the chemical synthesis of these peptide epitopes by SPPS, they can be coupled to protein carriers to develop efficient immunogens. Moreover, multiple antigenic peptides with a polylysine core can be designed and synthesized.This review focuses on the strategies developed to obtain synthetic immunogens for the production of antivenoms against the toxic Cys-rich peptides of scorpions and spiders.

Published
2020
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4. Protocol for bevacizumab purification using Ac-PHQGQHIGVSK-agarose

Author

Gabriela R. Barredo, Silvana L. Giudicessi, María C. Martínez Ceron, Soledad L. Saavedra, Santiago Rodríguez, Lucas Filgueira Risso, Rosa Erra-Balsells, Gustavo Mahler, Fernando Albericio, Osvaldo Cascone, and Silvia A. Camperi

Subjects
Peptide, Ligand, Downstream processing, Biopharmaceuticals, Monoclonal antibodies, Affinity chromatography, Science
Abstract

Bevacizumab is a monoclonal antibody, produced in CHO cells, used for the treatment of many human cancers. It is an anti-vascular endothelial growth factor (antsi-VEGF) that blocks the growth of tumor blood vessels. Nowadays its purification is achieved by affinity chromatography (AC) using protein A which is a very expensive ligand. On the other hand, the peptide Ac-PHQGQHIGVSK contained in the VEGF fragment binds bevacizumab with high affinity. This short peptide ligand has higher stability and lower cost than protein A and it can be prepared very easily by solid phase peptide synthesis. The present protocol describes the synthesis of Ac-PHQGQHIGVSK-agarose and its use for affinity chromatography purification of bevacizumab from a clarified CHO cell culture. • Ac-PHQGQHIGVSK-agarose capacity and selectivity are equivalent to those of protein A matrices. • The peptide ligand shows a greater stability and lower cost. The lack of Trp, Met or Cys in the peptide ligand prevents its oxidation and extends the useful life of the chromatographic matrix. • Mild conditions used during chromatography preserved the integrity of bevacizumab.

Published
2020
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5. Protocol for bevacizumab purification using Ac-PHQGQHIGVSK-agarose

Author

Fernando Albericio, Soledad L. Saavedra, Gustavo Mahler, Silvana L. Giudicessi, Gabriela R. Barredo, Santiago Rodríguez, Silvia A. Camperi, María C. Martínez Ceron, Lucas Filgueira Risso, Osvaldo Cascone, and Rosa Erra-Balsells

Subjects
medicine.drug_class, Otras Ciencias Biológicas, Clinical Biochemistry, Ligand, Peptide, 010501 environmental sciences, Affinity chromatography, Monoclonal antibody, 01 natural sciences, Biopharmaceuticals, Ciencias Biológicas, purl.org/becyt/ford/1 [https], 03 medical and health sciences, chemistry.chemical_compound, Biochemistry, Genetics and Molecular Biology, medicine, Peptide synthesis, lcsh:Science, Ligandos, purl.org/becyt/ford/1.6 [https], ComputingMethodologies_COMPUTERGRAPHICS, 030304 developmental biology, 0105 earth and related environmental sciences, chemistry.chemical_classification, mAb, 0303 health sciences, Downstream processing, biology, Péptidos, Ligand (biochemistry), Solid phase peptide synthesis, Medical Laboratory Technology, chemistry, Biochemistry, Afinidad, biology.protein, Agarose, Monoclonal antibodies, lcsh:Q, Protein A, Bevacizumab purification using Ac-PHQGQHIGVSK-agarose, CIENCIAS NATURALES Y EXACTAS
Abstract

Graphical abstract, Bevacizumab is a monoclonal antibody, produced in CHO cells, used for the treatment of many human cancers. It is an anti-vascular endothelial growth factor (antsi-VEGF) that blocks the growth of tumor blood vessels. Nowadays its purification is achieved by affinity chromatography (AC) using protein A which is a very expensive ligand. On the other hand, the peptide Ac-PHQGQHIGVSK contained in the VEGF fragment binds bevacizumab with high affinity. This short peptide ligand has higher stability and lower cost than protein A and it can be prepared very easily by solid phase peptide synthesis. The present protocol describes the synthesis of Ac-PHQGQHIGVSK-agarose and its use for affinity chromatography purification of bevacizumab from a clarified CHO cell culture. • Ac-PHQGQHIGVSK-agarose capacity and selectivity are equivalent to those of protein A matrices. • The peptide ligand shows a greater stability and lower cost. The lack of Trp, Met or Cys in the peptide ligand prevents its oxidation and extends the useful life of the chromatographic matrix. • Mild conditions used during chromatography preserved the integrity of bevacizumab.

Published
2019

6. Recombinant human follicle stimulating hormone purification by a short peptide affinity chromatography

Author

María C. Martínez Ceron, Juan M. Gurevich Messina, Silvia A. Camperi, Osvaldo Cascone, Guillermina Forno, Laura Mauro, Silvana L. Giudicessi, and Nicolás Urtasun

Subjects
0301 basic medicine, DOWNSTREAM PROCESSING, Peptide, CHO Cells, INGENIERÍAS Y TECNOLOGÍAS, 01 natural sciences, Biochemistry, Chromatography, Affinity, BIOPHARMACEUTICALS, Biotecnología Industrial, AFFINITY CHROMATOGRAPHY, 03 medical and health sciences, Cricetulus, Recombinant human follicle stimulating hormone, Affinity chromatography, Structural Biology, Drug Discovery, Animals, Humans, SOLID PHASE PEPTIDE SYNTHESIS, Molecular Biology, Pharmacology, chemistry.chemical_classification, Downstream processing, Protein Stability, Chemistry, 010401 analytical chemistry, Organic Chemistry, Acetylation, PEPTIDES, General Medicine, Molecular biology, Recombinant Proteins, 0104 chemical sciences, Immobilized Proteins, 030104 developmental biology, Molecular Medicine, Follicle Stimulating Hormone, Human, Peptides
Abstract

Peptide KVPLITVSKAK was selected to design a synthetic ligand for affinity chromatography purification of recombinant human follicle stimulating hormone (rhFSH), based on the interaction of the hormone with the exoloop 3 of its receptor. The peptide was acetylated to improve its stability to degradation by exopeptidases. A cysteine was incorporated at the C-termini to facilitate its immobilization to the chromatographic activated SulfoLink agarose resin. A sample of crude rhFSH was loaded to the affinity column, using 20 mM sodium phosphate, 0.5 mM methionine, and pH 5.6 and 7.2 as adsorption and elution buffers, respectively. The dynamic capacity of the matrix was 54.6 mg rhFSH/mL matrix and the purity 94%. The percentage of oxidized rhFSH was 3.4%, and that of the free subunits was 1.2%, both in the range established by the European Pharmacopeia, as also were the sialic acid content and the isoforms profile. Fil: Gurevich Messina, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Giudicessi, Silvana Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Martínez Ceron, María Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Urtasun, Nicolás. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Forno, Angela Guillermina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Mauro, Laura Valeria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Cascone, Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Camperi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina

Published
2018
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7. Single step recombinant human growth hormone (rhGH) purification from milk by peptide affinity chromatography

Author

Fernando Albericio, María C. Martínez Ceron, Soledad L. Saavedra, Osvaldo Cascone, Rosa Erra-Balsells, Silvia A. Camperi, Silvana L. Giudicessi, Guillermina Forno, María Belén Bosco, and Mariela M. Marani

Subjects
0301 basic medicine, Transgene, PEPTIDE LIGANDS, Protein Array Analysis, DOWNSTREAM PROCESSING, 030209 endocrinology & metabolism, Peptide, INGENIERÍAS Y TECNOLOGÍAS, Chromatography, Affinity, RECOMBINANT BIOPHARMACEUTICALS, law.invention, Biotecnología Industrial, 03 medical and health sciences, chemistry.chemical_compound, BIOLOGICS, 0302 clinical medicine, Affinity chromatography, law, Animals, Humans, chemistry.chemical_classification, Downstream processing, Chromatography, Human Growth Hormone, TRANSGENIC COW MILK, food and beverages, Recombinant Proteins, Amino acid, 030104 developmental biology, Milk, chemistry, Recombinant DNA, Agarose, Otras Biotecnología Industrial, SOLID-PHASE PEPTIDE SYNTHESIS, Biotechnology, Hormone
Abstract

Recombinant human growth hormone (rhGH) is used for the treatment of several pathologies, most of them related to growth. Although different expression systems can be used for its production, the milk from transgenic cows is one of the most interesting due to the high rhGH level achieved (5 g/L). We have designed and synthesized short peptides (9 or 10 amino acid long) using Fmoc chemistry and studied their ability to purify rhGH from milk once immobilized on an agarose support. Using spiked milk with the hormone as a sample, rhGH was purified with 88% yield and 92% purity in a single step with a fold purification of 4.5. Fil: Saavedra, Soledad Lorena. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Martínez Ceron, María Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Giudicessi, Silvana Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina Fil: Forno, Angela Guillermina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Bosco, Maria Belen. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Marani, Mariela Mirta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto Patagónico para el Estudio de los Ecosistemas Continentales; Argentina Fil: Erra Balsells, Rosa. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina Fil: Albericio Palomera, Fernando. Universidad de Barcelona; España Fil: Cascone, Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Camperi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina

Published
2018
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8. Friendly Strategy to Prepare Encoded One Bead−One Compound Cyclic Peptide Library

Author

María C. Martínez-Ceron, Silvana L. Giudicessi, Osvaldo Cascone, Rosa Erra-Balsells, Fernando Albericio, Juan M. Gurevich-Messina, and Silvia A. Camperi

Subjects
chemistry.chemical_classification, Físico-Química, Ciencia de los Polímeros, Electroquímica, Ciencias Químicas, Peptide, General Chemistry, General Medicine, Combinatorial chemistry, Peptides, Cyclic, Cyclic peptide, Solid-phase synthesis, 2-PHENYLISOPROPYL, Química Orgánica, Affinity chromatography, chemistry, Peptide Library, Side chain, Combinatorial Chemistry Techniques, MALDI-TOF MS/MS, PEPTIDE SEQUENCING, Target protein, Selectivity, Peptide library, COMBINATORIAL CHEMISTRY, CIENCIAS NATURALES Y EXACTAS, AFFINITY
Abstract

One bead−one peptide libraries allow the screening of suitable ligands for any target protein. Short cyclic peptides are ideal ligands for affinity chromatography because of their high affinity and selectivity for the target protein and stability against proteases. We designed a library synthesis strategy to facilitate the identification of cyclic peptides by MS consisting of (a) sequential incorporation of a mixture of Fmoc-Ala-OH and Fmoc-Asp[2-phenylisopropyl (OPp)]-OH (15:85) to Gly-oxymethylbenzamide-ChemMatrix (Gly-HMBA-CM) resin, (b) synthesis of the combinatorial library on the resin by the divide−couple−recombine method, (c) removal of OPp with 4% TFA, (d) peptide cyclization on solid phase through side-chain Asp and amino terminus, and (e) removal of side chain protecting groups with a 95% TFA cocktail. Peptides were cleaved from the beads with ammonia and the linear code was sequenced by MALDI-TOF MS/MS. The high capacity of ChemMatrix resin together with the sensitivity of MS allows code sequencing from a single bead. Fil: Giudicessi, Silvana Laura. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Gurevich Messina, Juan Manuel. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina; Fil: Martínez Ceron, María Camila. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Erra Balsells, Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Albericio, F.. Instituto de Investigación Biomédica; España; Universidad de Barcelona; España; Centro de Investigación Biomédica en Red en Bioingeniería, Biomateriales y Nanomedicina; España; Fil: Cascone, Osvaldo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina; Fil: Camperi, Silvia Andrea. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina

Published
2013
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9. Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest

Author

Silvia A. Camperi, F.J. Wolman, Mariano Grasselli, A.A.N. Cañizo, O. Cascone, and Nancy B. Iannucci

Subjects
chemistry.chemical_classification, pseudobiospecific ligands, Chromatography, Iminodiacetic acid, General Chemical Engineering, lcsh:TP155-156, chemistry.chemical_element, Fractionation, Copper, chemistry.chemical_compound, affinity chromatography, Membrane, Enzyme, chemistry, Affinity chromatography, protein purification, Protein purification, Agarose, lcsh:Chemical engineering
Abstract

High-performance affinity matrices were obtained by attaching pseudobiospecific ligands to hollow-fibre membranes. The neutral protease contained in FlavourzymeTM was purified to homogeneity with Yellow 4R-HE affinity hollow-fibre membranes. Immobilisation of Red HE-3B allowed purification of a milk-clotting enzyme obtained by solid-state culture of Mucor bacilliformis. Copper immobilisation through iminodiacetic acid allowed fractionation of Biocon Bioconcentrated PlusTM to separate the pectinesterase-containing fraction. The productivity of the developed processes - 1900, 94 and 750 U/ml.min, respectively - was 10- to 15-fold higher than that achieved with the same ligands immobilised on agarose-based soft gels, mainly due to the shortening of the purification processes.

Published
2003

10. Screening of One-Bead-One-Peptide Combinatorial Library Using Red Fluorescent Dyes. Presence of Positive and False Positive Beads.

Author

Mariela M. Marani, María C. Martínez Ceron, Silvana L. Giudicessi, Eliandre de Oliveira, Simon Côté, Rosa Erra-Balsells, Fernando Albericio, Osvaldo Cascone, and Silvia A. Camperi

Subjects
*PEPTIDES, *STREPTAVIDIN, *FLUORESCENCE, *MASS spectrometry
Abstract

To screen one-bead-one-compound (OBOC) combinatorial libraries, tens of thousands to millions of compound beads are first mixed with a target molecule. The beads that interact with this molecule are then identified and isolated for compound structure determination. Here we describe an OBOC peptide library screening using streptavidin (SA) as probe protein, labeled with a red fluorescent dye and using the COPAS BIO-BEAD flow sorting equipment to separate fluorescent from nonfluorescent beads. The red dyes used were ATTO 590 and Texas Red. After incubating the library with the SA-red fluorescent dye conjugate, we isolated positive beads caused by peptide-SA interaction and false positive beads produced by peptide-fluorescent dye interaction. These false positives were a drawback when sorting beads by COPAS. However, an in depth analysis of both kinds of beads allowed the differentiation of positives from false positives. The false positive beads showed bright homogeneous fluorescence, while positive beads had a heterogeneous fluorescence, exhibiting a characteristic halo appearance, with fluorescence intensity greatest at the bead surface and lowest in the core. The difference was more evident when using Texas Red instead of ATTO 590. Thus, positive beads could be manually separated from false positive ones. The beads were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). Most of the sequences obtained from positive beads had the His-Pro-Gln motif. Peptides from false positive beads were rich in Leu/Ileu, His, Phe, and Tyr. [ABSTRACT FROM AUTHOR]

Published
2009
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11. From the One-Bead-One-Compound Concept to One-Bead-One-Reactor.

Author

Mariela M. Marani, Marta Paradís-Bas, Judit Tulla-Puche, Simón Côté, Silvia A. Camperi, Osvaldo Cascone, and Fernando Albericio

Subjects
*ORGANIC compounds, *CARBON compounds, *ORGANIC chemistry, *PEPTIDES
Abstract

The one-bead-one-compound method gives access to millions of compounds that can be screened directly on the bead. Although characterization techniques are increasingly potent and reliable, problems can still be encountered in deciphering the sequence of the active compound because of sensitiveness or manipulation of the bead. ChemMatrix, a totally PEG-based resin, has resolved the synthesis of peptides of outstanding difficulty. Like other PEG-based resins, it permits on-bead screening because of its compatibility in aqueous media and has the further advantage of having a high loading, comparable to polystyrene resins. ChemMatrix beads previously swelled in water can be nicely divided into four parts that can be characterized using different analytical techniques or just stored for safety or for further testing. The four bead parts show high homogeneity and can thus be considered to be replicas. [ABSTRACT FROM AUTHOR]

Published
2007
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