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1. 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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2. Las Tecnologías y la Enseñanza en la Educación Superior. Un Simulador Aplicado a la Integración de Conceptos Enseñados en Cursos de Posgrado

Author

Silvana L. Giudicessi, María C. Martínez-Ceron, Soledad L. Saavedra, Osvaldo Cascone, and Silvia A. Camperi

Subjects
Education, Special aspects of education, LC8-6691
Abstract

Introducción: El objetivo de este trabajo fue implementar tecnologías de la información y la comunicación (TIC) a nivel de posgrado. En este caso particular se usó USINA, un simulador para la toma de decisiones diseñado por el Centro de Innovaciones en Tecnología y Pedagogía (CITEP), de la Universidad de Buenos Aires. Ésta permite trabajar con narraciones, estudio de casos y utilizar el “error” como método pedagógico. Métodos: 1) Diseñar una secuencia de pantallas para ser montadas en USINA utilizándola como herramienta de integración de conceptos en dos cursos de posgrado: Downstream Processing de proteínas (DSP) y Aplicaciones, Síntesis y Análisis de Péptidos Sintéticos (ASAP). 2) Aplicar una encuesta anónima para evaluar la eficiencia de USINA. 3) Realizar una clase presencial para intercambiar opiniones sobre la experiencia. Resultados y Discusión: En ambos cursos (DSP y ASAP) la experiencia resultó exitosa. El alumnado consideró que el uso de USINA permitió el andamiaje de conocimientos y la integración de conceptos al situarlo en el rol de experto. El uso de las TIC en los niveles educativos superiores sigue siendo una asignatura pendiente. A través de la experiencia aquí analizada, se abre la posibilidad de llevar esta herramienta a cursos de pregrado y con mayor número de estudiantes.Palabras clave: Simulador, Tecnología de la educación, Enseñanza superior, Integración, Biotecnología, Química, Tecnologías de la información y de la comunicación, Enseñanza-aprendizaje, Innovación pedagógica. Technology and Teaching in Higher Education. A Simulation Applied to the Integration of Concepts Taught in Postgraduate CoursesIntroduction: The aim of this work was to implement information and communication technologies (ICTs) at postgraduate level. In this particular case, USINA, a decision-making simulator designed by the Center for Innovation in Technology and Education (CITEP), of the University of Buenos Aires, was used. It allows working with stories, case studies and uses the "error" as a teaching method. Methods: 1) Design a sequence of screens to be mounted in the USINA platform to use it as a tool for the integration of concepts in two postgraduate courses: Protein Downstream Processing (DSP) and Applications, Synthesis and Analysis of Synthetic Peptides (ASAP). 2) Apply anonymous quiz to evaluate the efficiency of USINA. 3) Perform a class attendance to exchange opinions on the experience. Results: During both courses (DSP and ASAP) the experience was very successful. The students felt that the use of USINA enhanced learning and helped integrating concepts by situating them in the role of experts. Discussion: The use of ICTs in higher levels of education remains a pending issue. Through the experience here analyzed the possibility to bring this tool to undergraduate courses and more students is opened.Keywords: Simulation, Educational technology, Higher education, Integration, Biotechnology, Chemistry, Information and communication technologies, Teaching-learning, Educational innovation.

Published
2016
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3. Contributors

Author

Ali Abbas, Mohd Azmuddin Abdullah, Ifeyinwa C. Adaka, F.S. Aguiar, I.Q.S. Aguiar, Mushtaq Ahmad, Giselle Cristine Melo Aires, Nisar Akbar, Abida Akram, Ahmed Al Otaibi, Fernando Albericio, Shifaqat Ali, Omar Mahmoud Said Alshajrawi, Aamir H. Bhat, Silvia A. Camperi, Alejandra B. Cardillo, Raul Nunes de Carvalho, Osvaldo Cascone, Ahmad Cheikhyoussef, Natascha Cheikhyoussef, Gun Hean Chong, Wanessa Almeida da Costa, Ivonete Quaresma da Silva, Luiza Helena da Silva Martins, Maria Caroline Rodrigues Ferreira, Umaima Gazal, Silvana L. Giudicessi, Sandra Gonçalves, Ashanul Haque, Amir Hussain, Erum Akbar Hussain, Hanaa Ali Hussein, Imran Khan, Mohd Wajid Ali Khan, Omer Kilic, Sangeetha Kumaravel, Subrata Kundu, Sin Yee Lee, María C. Martínez Ceron, Eduardo Gama Ortiz Menezes, Syed Ali Raza Naqvi, Joicy Corrêa de Oliveira, Vishal Pathak, Parmita Phukan, A.S.O. Pinto, Flávia Cristina Seabra Pires, Thatiana Mendonça Ribeiro, H.L.G. Rogez, Anabela Romano, Soledad L. Saavedra, Diganta Sarma, Syed Muhammad Ali Shah, Gorkem Deniz Sonmez, Ana Paula de Souza e Silva, Shazia Sultana, L.E.O. Teixeira, Prabaharan Thiruvengetam, Philip F. Uzor, Ghulam Yaseen, and Muhammad Zafar

Published
2021
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4. Green solvents in the biotechnology-based pharmaceutical industry

Author

Fernando Albericio, Osvaldo Cascone, María C. Martínez Ceron, Soledad L. Saavedra, Silvana L. Giudicessi, Alejandra B. Cardillo, and Silvia A. Camperi

Subjects
Exploit, business.industry, Fossil fuel, Environmental impact assessment, business, Toxic chemical, Non-renewable resource, Biotechnology, Pharmaceutical industry
Abstract

After the Industrial Revolution, humanity began to exploit nonrenewable resources, such as oil and gas, with dangerous consequences for the environment. In the last 50 years, different strategies have been implemented to reduce the environmental impact produced by the chemical and pharmaceutical industries. Biotechnology offers different perspectives, such as the use of biocatalysts, microorganisms, or plant/animal cells (or parts thereof) to replace highly toxic chemical processes. On the other hand, different methodologies are used during the purification processes of drugs and biopharmaceuticals. One of the most used is affinity chromatography, which consists of having a column of a matrix with an anchored ligand that recognizes the product of interest. The use of greener alternatives is a commitment for both the developed and developing countries.

Published
2021
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5. Design of Affinity Chromatography Peptide Ligands Through Combinatorial Peptide Library Screening

Author

Soledad L. Saavedra, Gabriela R. Barredo, María C. Martínez-Ceron, Fernando Albericio, Silvana L. Giudicessi, Silvia A. Camperi, Osvaldo Cascone, and Mariela M. Marani

Subjects
chemistry.chemical_classification, Chromatography, 010405 organic chemistry, Chemistry, Peptide, 010402 general chemistry, Mass spectrometry, Tandem mass spectrometry, 01 natural sciences, 0104 chemical sciences, Adsorption, Affinity chromatography, Protein purification, Target protein, Peptide library
Abstract

In this chapter, a protocol to design affinity chromatography matrices with short peptide ligands immobilized for protein purification is described. The first step consists of the synthesis of a combinatorial peptide library on the hydroxymethylbenzoyl (HMBA)-ChemMatrix resin by the divide-couple-recombine (DCR) method using the Fmoc chemistry. Next, the library is screened with the protein of interest labeled with a fluorescent dye or biotin. Subsequently, peptides contained on positive beads are identified by tandem matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS/MS), and those sequences showing greater consensus are synthesized in larger quantities and immobilized on chromatographic supports. Finally, target protein adsorption on peptide affinity matrices is evaluated through equilibrium adsorption isotherms and breakthrough curves.

Published
2020
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6. Development of a hyperimmune equine serum therapy for COVID-19 in Argentina

Author

Vanesa Zylberman, Santiago Sanguineti, Andrea V. Pontoriero, Sandra V. Higa, María L. Cerutti, Susana M. Morrone Seijo, Romina Pardo, Luciana Muñoz, María E. Acuña Intrieri, Vanina A. Alzogaray, Martín M. Avaro, Estefanía Benedetti, Paula M. Berguer, Laura Bocanera, Lucas Bukata, Marina S. Bustelo, Ana M. Campos, Mariana Colonna, Elisa Correa, Lucía Cragnaz, María E. Dattero, María Dellafiore, Sabrina Foscaldi, Joaquín V. González, Luciano L. Guerra, Sebastián Klinke, María S. Labanda, Constanza Lauché, Juan C. López, Anabela M. Martínez, Lisandro H. Otero, Elías H. Peyric, Pablo F. Ponziani, Romina Ramondino, Jimena Rinaldi, Santiago Rodríguez, Javier E. Russo, Mara L. Russo, Soledad L. Saavedra, Mauricio Seigelchifer, Santiago Sosa, Claudio Vilariño, Patricia López Biscayart, Esteban Corley, Linus Spatz, Elsa G. Baumeister, and Fernando A. Goldbaum

Subjects
lcsh:Immunologic diseases. Allergy, Pneumonia, Viral, Argentina, lcsh:Medicine, f(ab')2 fragments, Antibodies, Viral, lcsh:Infectious and parasitic diseases, Betacoronavirus, Immunoglobulin Fab Fragments, Neutralization Tests, Animals, Humans, lcsh:RC109-216, Horses, Pandemics, COVID-19 Serotherapy, SARS-CoV-2, Immune Sera, lcsh:R, Immunization, Passive, COVID-19, Immunoglobulin G, Spike Glycoprotein, Coronavirus, lcsh:RC581-607, Coronavirus Infections, hyperimmune horse sera
Abstract

The disease named COVID-19, caused by the SARS-CoV-2 coronavirus, is currently generating a global pandemic. Vaccine development is no doubt the best long-term immunological approach, but in the current epidemiologic and health emergency there is a need for rapid and effective solutions. Convalescent plasma is the only antibody-based therapy available for COVID-19 patients to date. Equine polyclonal antibodies (EpAbs) put forward a sound alternative. The new generation of processed and purified EpAbs containing highly purified F(ab')2 fragments demonstrated to be safe and well tolerated. EpAbs are easy to manufacture allowing a fast development and scaling up for a treatment. Based on these ideas, we present a new therapeutic product obtained after immunization of horses with the receptor-binding domain of the viral Spike glycoprotein. Our product shows around 50 times more potency in in vitro seroneutralization assays than the average of convalescent plasma. This result may allow us to test the safety and efficacy of this product in a phase 2/3 clinical trial to be conducted in July 2020 in the metropolitan area of Buenos Aires, Argentina.La enfermedad denominada COVID-19 es causada por el coronavirus SARS-CoV-2 y es actualmente considerada una pandemia a nivel global. El desarrollo de vacunas es sin duda la mejor estrategia a largo plazo, pero debido a la emergencia sanitaria, existe una necesidad urgente de encontrar soluciones rápidas y efectivas para el tratamiento de la enfermedad. Hasta la fecha, el uso de plasma de convalecientes es la única inmunoterapia disponible para pacientes hospitalizados con COVID-19. El uso de anticuerpos policlonales equinos (EpAbs) es otra alternativa terapéutica interesante. La nueva generación de EpAbs incluyen el procesamiento y purificación de los mismos y la obtención de fragmentos F(ab')2 con alta pureza y un excelente perfil de seguridad en humanos. Los EpAbs son fáciles de producir, lo cual permite el desarrollo rápido y la elaboración a gran escala de un producto terapéutico. En este trabajo mostramos el desarrollo de un suero terapéutico obtenido luego de la inmunización de caballos utilizando el receptor-binding domain de la glicoproteína Spike del virus. Nuestro producto mostró ser alrededor de 50 veces más potente en ensayos de seroneutralización in vitro que el promedio de los plasmas de convalecientes. Estos resultados nos permitirían testear la seguridad y eficacia de nuestro producto en ensayos clínicos de fase 2/3 a realizarse a partir de julio de 2020 en la zona metropolitana de Buenos Aires, Argentina.

Published
2020

7. Natural Snake Venom Inhibitors and their Pharmaceutical Uses: Challenges and Possibilities

Author

Lucia Avila, Silvia A. Camperi, Soledad L. Saavedra, Fernando Albericio, Silvana L. Giudicessi, María C. Martínez-Ceron, and Osvaldo Cascone

Subjects
0301 basic medicine, Pharmacology, Biological Products, Traditional medicine, Antivenins, business.industry, 030106 microbiology, Antivenom, Venom, complex mixtures, World health, 03 medical and health sciences, Snake venom, Drug Discovery, Animals, Humans, Medicine, business, Snake Venoms
Abstract

Nowadays, treatment with specific antivenins is considered the only cure for snakebites accidents. However, access to antivenom obstructs the successful implementation of the World Health Organization international guidelines. In the last few years, natural organic compounds, peptides, and proteins with the ability to inhibit snake toxins and obtained from different sources such as plant extracts and animal blood have been proposed as antivenoms. In this work, we will focus on the inhibitors of the main venom toxins, phospholipases A2 and metalloproteinases, and their application as novel antivenoms.

Published
2018
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8. Simple method to assess stability of immobilized peptide ligands against proteases

Author

María L. Salum, María C. Martínez-Ceron, Osvaldo Cascone, Soledad L. Saavedra, Rosa Erra-Balsells, Silvia A. Camperi, and Silvana L. Giudicessi

Subjects
Pharmacology, chemistry.chemical_classification, Proteases, Chromatography, Protein mass spectrometry, 010405 organic chemistry, Chemistry, Electrospray ionization, 010401 analytical chemistry, Organic Chemistry, Peptide, General Medicine, Mass spectrometry, 01 natural sciences, Biochemistry, Combinatorial chemistry, 0104 chemical sciences, Amino acid, Affinity chromatography, Structural Biology, Desorption, Drug Discovery, Molecular Medicine, Molecular Biology
Abstract

Although peptides are used as affinity chromatography ligands, they could be digested by proteases. Usually, peptide stability is evaluated in solution, which differs from the resin-bounded peptide behavior. Furthermore, the study of the degradation products requires purification steps before analysis. Here, we describe an easy method to assess immobilized peptide stability. Sample peptides were synthesized on hydroxymethylbenzamide-ChemMatrix resin. Peptidyl-resin beads were then incubated with solutions containing proteases. Peptides were detached from the solid support with ammonia vapor and analyzed by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry, allowing the detection of the whole peptides as well as their C-terminal degradation products. The method allowed a fast evaluation of peptide ligand stability in solid phase towards proteases that may be present in the crude sample before their use as ligands in affinity chromatography. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

Published
2017
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9. 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

10. Use of a phosphopeptide as a ligand to purify phospholipase A

Author

Soledad L, Saavedra, Gerardo, Acosta, Lucía, Ávila, Silvana L, Giudicessi, Silvia A, Camperi, Fernando, Albericio, Osvaldo, Cascone, and María C, Martínez Ceron

Subjects
Phosphopeptides, Phospholipases A2, Sepharose, Crotalid Venoms, Crotalus, Animals, Succinimides, Crotoxin, Ligands, Amides, Chromatography, Affinity, Mass Spectrometry, Solid-Phase Synthesis Techniques
Abstract

The venom of Crotalus durissus terrificus (Cdt) is a source of a wide variety of toxins, some of them with interesting pharmacological applications. Of these toxins, the phospholipase A

Published
2019

11. A short peptide fragment of the vascular endothelial growth factor as a novel ligand for bevacizumab purification

Author

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

Subjects
0106 biological sciences, Vascular Endothelial Growth Factor A, medicine.drug_class, Surface Properties, Chemistry, Pharmaceutical, Peptide, Antineoplastic Agents, INGENIERÍAS Y TECNOLOGÍAS, CHO Cells, Monoclonal antibody, Ligands, 01 natural sciences, biofármacos, Chromatography, Affinity, Biotecnología Industrial, 03 medical and health sciences, chemistry.chemical_compound, Cricetulus, Affinity chromatography, Drug Stability, 010608 biotechnology, medicine, Animals, Humans, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Chromatography, biology, Sepharose, péptídos, Peptide Fragments, Vascular endothelial growth factor, Dissociation constant, Bevacizumab, Immobilized Proteins, chemistry, anticuerpo, biology.protein, Agarose, Purificación, Protein A, Chromatography column, Biotechnology, Protein Binding
Abstract

Bevacizumab is a vascular endothelial growth factor (VEGF)-directed monoclonal antibody (mAb) used for the treatment of several human cancers. Given that bevacizumab is administered intravenously, it must have extremely high purity, which is achieved by purification with protein A affinity chromatography (AC). However, protein A is a very expensive ligand, thereby increasing the cost of purification. Furthermore, the harsh elution conditions required to recover bevacizumab from the AC column can damage both the mAb and protein A. In contrast, short peptides show higher stability, easier synthesis and lower cost and are therefore ideal ligands for AC. In the present study, the peptide Ac-PHQGQHIGVSK contained in the VEGF fragment that binds bevacizumab, was synthesized and immobilized on agarose. The peptidyl-agarose showed affinity for bevacizumab, with an equilibrium dissociation constant value of 2.20.5 x 10−7 M under optimal conditions. Samples of CHO cell filtrate producing bevacizumab were loaded on the peptidyl-agarose chromatography column. Bevacizumab was recovered from the elution fraction with a yield of 94% and a purity of 98%. The maximum capacity (qm) 382 mg of bevacizumab per mL of matrix was comparable to that of commercial protein A matrices. Moreover, the peptide ligand showed greater stability and a lower cost than protein A. Unlike peptides previously reported for IgG purification, the ligand described herein allows mAb elution under mild conditions, thereby favoring the integrity of bevacizumab. The lack of Trp, Met or Cys in the peptide prevents its oxidation and extends the useful life of the chromatographic matrix. Fil: Barredo, Gabriela Romina. 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: Saavedra, Soledad Lorena. 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: Rodriguez, Santiago. No especifíca; Fil: Filgueira Risso, Lucas. No especifíca; 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: Mahler, Gustavo. No especifíca; Fil: Albericio, Fernando. University of KwaZulu-Natal; Sudáfrica 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
2019

12. Combinatorial Library Screening Coupled to Mass Spectrometry to Identify Valuable Cyclic Peptides

Author

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

Subjects
Peptide, 010402 general chemistry, Mass spectrometry, Peptides, Cyclic, 01 natural sciences, Mass Spectrometry, CYCLIC PEPTIDES, MALDI-MS, chemistry.chemical_compound, Peptide Library, Amino Acid Sequence, Peptide library, Peptide sequence, Glycolic acid, Depsipeptide, chemistry.chemical_classification, 010405 organic chemistry, Otras Ciencias Químicas, Ciencias Químicas, PEPTIDES, General Medicine, Combinatorial chemistry, Cyclic peptide, 0104 chemical sciences, chemistry, SYNTHESIS CYLIC PEPTIDES, Linker, CIENCIAS NATURALES Y EXACTAS
Abstract

Combinatorial library screening coupled to mass spectrometry (MS) analysis isa practical approach to identify useful peptides. Cyclic peptides can have highbiological activity, selectivity, and affinity for target proteins, and high stabilityagainst proteolytic degradation. Here we describe two strategies to preparecombinatorial libraries suitable for MS analysis to accelerate the discoveryof cyclic peptide structures. Both approaches use ChemMatrix resin and thelinker 4-hydroxymethylbenzoic acid. One strategy involves the synthesis ofa one-bead?two-peptides library in which each bead contains both the cyclicpeptide and its linear counterpart to facilitate MS analysis. The other protocol isbased on the synthesis of a cyclic depsipeptide library in which a glycolamidicester group is incorporated by adding glycolic acid. After library screening, thering is opened and the peptide is released simultaneously for subsequent MSanalysis. 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 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: 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: Saavedra, Soledad Lorena. 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: Acosta, Gerardo. Universidad de Barcelona; España. Consorcio Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; 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: Erra Balsells, Rosa. 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. Consorcio Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España

Published
2016
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13. Latest Advances in OBOC Peptide Libraries. Improvements in Screening Strategies and Enlarging the Family From Linear to Cyclic Libraries

Author

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

Subjects
Computer science, Pharmaceutical Science, Peptide, PEPTIDE LIBRARY, INGENIERÍAS Y TECNOLOGÍAS, Ligands, 010402 general chemistry, Peptides, Cyclic, 01 natural sciences, chemistry.chemical_compound, Peptide Library, Tandem Mass Spectrometry, Screening method, Humans, Peptide library, CYCLIC PEPTIDE, One bead one compound, chemistry.chemical_classification, 010405 organic chemistry, Peptoid, Combinatorial chemistry, Cyclic peptide, 0104 chemical sciences, Ingeniería Química, chemistry, Otras Ingeniería Química, PEPTOID, MALDI TOF MSMS, Biotechnology, Enzymatic degradation
Abstract

Solid phase screenings of one bead one compound (OBOC) libraries have been widely used to find ligands with pharmacological and analytical uses, and to purify or detect proteins in complex mixtures. To improve library screening, in the last years various strategies have been developed to avoid the selection of false positive beads and to obtain selective ligands. Currently, there is great interest in cyclic peptides because of their resistance to enzymatic degradation and higher selectivity compared to their linear counterparts. Lots of cyclic peptide libraries protocols have been recently developed to facilitate hits analysis. The aim of this review is to summarize the latest applications of solid phase screening of OBOC combinatorial peptide libraries, the improvements in the screening methods including mass spectrometry MS/MS techniques and the strategies to synthesize OBOC cyclic peptide libraries 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. 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: Saavedra, Soledad Lorena. 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: 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: Erra Balsells, Rosa. 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. Instituto de Ciencia y Tecnología de Barcelona; España. Universidad de Barcelona; España. Parque Científico de Barcelona; España. Universidad de Kwazulu; Sudáfrica 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. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”; 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
2016
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14. Use of a phosphopeptide as a ligand to purify phospholipase A2 from the venom of Crotalus durisuss terrificus by affinity chromatography

Author

Lucía Ávila, Silvana L. Giudicessi, Osvaldo Cascone, Gerardo A. Acosta, Fernando Albericio, Soledad L. Saavedra, María Camila Martínez Ceron, and Silvia A. Camperi

Subjects
Chromatography, biology, Chemistry, Phosphopeptide, 010401 analytical chemistry, Clinical Biochemistry, Crotalus, Venom, Cell Biology, General Medicine, biology.organism_classification, 030226 pharmacology & pharmacy, 01 natural sciences, Biochemistry, 0104 chemical sciences, Analytical Chemistry, Crotamine, 03 medical and health sciences, 0302 clinical medicine, Phospholipase A2, Affinity chromatography, Snake venom, biology.protein, lipids (amino acids, peptides, and proteins), Antibacterial agent
Abstract

The venom of Crotalus durissus terrificus (Cdt) is a source of a wide variety of toxins, some of them with interesting pharmacological applications. Of these toxins, the phospholipase A2 (PLA2) subunit of crotoxin (Ctx) has been studied for its potential as an antiviral and antibacterial agent. Peptides have proven useful ligands for the purification of numerous molecules, including antibodies, toxins, enzymes and other proteins. Here, we sought to use a phosphopeptide (P-Lys) as a ligand for PLA2 purification. P-Lys was synthesized in solid phase on Rink-Amide-ChemMatrix resin, immobilized on NHS-agarose, and then evaluated as a chromatographic matrix. Under the best conditions, total protein adsorption reached 39% and only the eluate fraction presented PLA2 activity. Analysis of the eluate by SDS-PAGE showed three bands, one corresponding to the molecular weight of PLA2 (14 kDa). Said bands were analyzed by mass spectrometry and identified as PLA2 and its multimers. The final product showed a purity of over 90%. In addition, slightly changing the process conditions also allowed the isolation of crotamine.

Published
2020
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16. 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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17. Bevacizumab Purification by Peptide Affinity Chromatography

Author

Gabriela R. Barredo, Gustavo Mahler, Silvana L. Giudicessi, Soledad L. Saavedra, Mara C. Martnez-Ceron, Silvia A. Camperi, Fernando Albericio, and Osvaldo Cascone

Subjects
chemistry.chemical_classification, Chromatography, Bevacizumab, Affinity chromatography, Chemistry, medicine, Peptide, medicine.drug
Published
2018
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18. Targeted anti-inflammatory peptide delivery in injured endothelial cells using dermatan sulfate/chitosan nanomaterials

Author

Silvia A. Camperi, Juan Manuel Lázaro-Martínez, Romina Julieta Glisoni, Florencia Funez, Ariadna M. Birocco, Alejandro Sosnik, Agustín Blachman, Graciela C. Calabrese, and Soledad L. Saavedra

Subjects
Polymers and Plastics, Endothelium, media_common.quotation_subject, Population, POLYELECTROLYTE COMPLEX, Anti-Inflammatory Agents, Dermatan Sulfate, 02 engineering and technology, Tripeptide, 010402 general chemistry, 01 natural sciences, Dermatan sulfate, Ciencias Biológicas, Chitosan, Mice, chemistry.chemical_compound, ENDOTHELIAL CELLS, Human Umbilical Vein Endothelial Cells, Materials Chemistry, Fluorescence microscope, medicine, Animals, Humans, Internalization, education, CHITOSAN, Cells, Cultured, media_common, education.field_of_study, ANTI-INFLAMMATORY PEPTIDE, DERMATAN SULFATE, Organic Chemistry, Bioquímica y Biología Molecular, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Drug Liberation, Hyaluronan Receptors, medicine.anatomical_structure, chemistry, Biophysics, Nanoparticles, Nanomedicine, 0210 nano-technology, Oligopeptides, CIENCIAS NATURALES Y EXACTAS, Protein Binding
Abstract

This work describes a novel delivery system for targeting egg-derived anti-inflammatory tripeptide Ile-Arg-Trp (IRW) to endothelial cells. The nanomedicine is synthesized by a simple and reproducible ionotropic gelification method that results in the efficient loading of the positively charged IRW within the dermatan sulfate/ chitosan matrix, as demonstrated by ss-NMR spectroscopy. The incorporation of IRW results in a stable nanoparticle dispersion with a single size population of 442 ± 43 nm. Fluorescence microscopy studies demonstrate the capacity of the nanomaterial to distinguish between a quiescent and an injured endothelium through the interaction of dermatan sulfate with the CD44 receptor. Remarkably, no additional surface functionalization is required as dermatan sulfate mediates their internalization and the intracellular release of this natural anti-inflammatory tripeptide to modulate endothelial inflammatory response. This simple, scalable, and versatile nanotechnology platform opens new opportunities to apply in the therapy of vascular disease. Fil: Blachman, Agustín. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina Fil: Funez, Florencia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina Fil: Birocco, Ariadna María. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina Fil: Saavedra, Soledad Lorena. 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: Lazaro Martinez, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; 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 Fil: Glisoni, Romina Julieta. 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: Sosnik, Alejandro Dario. 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: Calabrese, Graciela Cristina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas; Argentina

Published
2020
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19. Simple method to assess stability of immobilized peptide ligands against proteases

Author

Silvana L, Giudicessi, María L, Salum, Soledad L, Saavedra, María C, Martínez-Ceron, Osvaldo, Cascone, Rosa, Erra-Balsells, and Silvia A, Camperi

Subjects
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Peptides, Chromatography, Affinity, Peptide Hydrolases
Abstract

Although peptides are used as affinity chromatography ligands, they could be digested by proteases. Usually, peptide stability is evaluated in solution, which differs from the resin-bounded peptide behavior. Furthermore, the study of the degradation products requires purification steps before analysis. Here, we describe an easy method to assess immobilized peptide stability. Sample peptides were synthesized on hydroxymethylbenzamide-ChemMatrix resin. Peptidyl-resin beads were then incubated with solutions containing proteases. Peptides were detached from the solid support with ammonia vapor and analyzed by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry, allowing the detection of the whole peptides as well as their C-terminal degradation products. The method allowed a fast evaluation of peptide ligand stability in solid phase towards proteases that may be present in the crude sample before their use as ligands in affinity chromatography. Copyright © 2017 European Peptide Society and John WileySons, Ltd.

Published
2017

20. Technology and Teaching in Higher Education. A Simulation Applied to the Integration of Concepts Taught in Postgraduate Courses

Author

María C. Martínez-Ceron, Soledad L. Saavedra, Silvia A. Camperi, Osvaldo Cascone, and Silvana L. Giudicessi

Subjects
0301 basic medicine, Biotecnología, Educación, Ciencias de la Educación, purl.org/becyt/ford/5.3 [https], CIENCIAS SOCIALES, 03 medical and health sciences, QUÍMICA ORGÁNICA, SIMULADORES, Enseñanza superior, Sociology, TIC, lcsh:LC8-6691, purl.org/becyt/ford/5 [https], lcsh:Special aspects of education, EDUCACIundefinedN EN BIOTECNOLOGundefinedA, Tecnología de la educación, 05 social sciences, Simulador, PundefinedPTIDOS SINTundefinedTICOS, 050301 education, Química, General Medicine, Tecnologías de la información y de la comunicación, PLATAFORMA VIRTUAL, Enseñanza-aprendizaje, 030104 developmental biology, Otras Ciencias de la Educación, ICTS, Innovación pedagógica, Integración, Postgraduate level, lcsh:L, 0503 education, Humanities, lcsh:Education
Abstract

Introducción: El objetivo de este trabajo fue implementar tecnologías de la información y la comunicación (TIC) a nivel de posgrado. En este caso particular se usó USINA, un simulador para la toma de decisiones diseñado por el Centro de Innovaciones en Tecnología y Pedagogía (CITEP), de la Universidad de Buenos Aires. Ésta permite trabajar con narraciones, estudio de casos y utilizar el “error” como método pedagógico. Métodos: 1) Diseñar una secuencia de pantallas para ser montadas en USINA utilizándola como herramienta de integración de conceptos en dos cursos de posgrado: Downstream Processing de proteínas (DSP) y Aplicaciones, Síntesis y Análisis de Péptidos Sintéticos (ASAP). 2) Aplicar una encuesta anónima para evaluar la eficiencia de USINA. 3) Realizar una clase presencial para intercambiar opiniones sobre la experiencia. Resultados y Discusión: En ambos cursos (DSP y ASAP) la experiencia resultó exitosa. El alumnado consideró que el uso de USINA permitió el andamiaje de conocimientos y la integración de conceptos al situarlo en el rol de experto. El uso de las TIC en los niveles educativos superiores sigue siendo una asignatura pendiente. A través de la experiencia aquí analizada, se abre la posibilidad de llevar esta herramienta a cursos de pregrado y con mayor número de estudiantes, Introduction: The aim of this work was to implement information and communication technologies (ICTs) at postgraduate level. In this particular case, USINA, a decision-making simulator designed by the Center for Innovation in Technology and Education (CITEP), of the University of Buenos Aires, was used. It allows working with stories, case studies and uses the "error" as a teaching method. Methods: 1) Design a sequence of screens to be mounted in the USINA platform to use it as a tool for the integration of concepts in two postgraduate courses: Protein Downstream Processing (DSP) and Applications, Synthesis and Analysis of Synthetic Peptides (ASAP). 2) Apply anonymous quiz to evaluate the efficiency of USINA. 3) Perform a class attendance to exchange opinions on the experience. Results: During both courses (DSP and ASAP) the experience was very successful. The students felt that the use of USINA enhanced learning and helped integrating concepts by situating them in the role of experts. Discussion: The use of ICTs in higher levels of education remains a pending issue. Through the experience here analyzed the possibility to bring this tool to undergraduate courses and more students is opened

Published
2016

21. One-Bead-One-Peptide Library to Purify Crotalus durissus terrificus Phosholipase A2

Author

Silvana L. Giudicessi, María C. Martínez-Ceron, Soledad L. Saavedra, Osvaldo Cascone, Silvia A. Camperi, Lucía Ávila, and Fernando Albericio

Subjects
Bead (woodworking), media_common.quotation_subject, Library science, Art, Peptide library, Crotalus durissus terrificus, media_common
Abstract

Maria C. Martinez-Ceron, Soledad L. Saavedra, Lucia Avila, Silvana L. Giudicessi, Fernando Albericio, Silvia A. Camperi and Osvaldo Cascone NANOBIOTEC Institute, UBA-CONICET, Cathedra of Biotechnology, School of Pharmacy and Biochemistry, UBA, CABA, 1113, Argentina; National Institute of Biologicals Production, ANLIS-Malbran, CABA, 1281, Argentina; IRB-PCB, UB. Barcelona, 08028, Spain; School of Chemistry, Yachay Tech, Yachay City of Knowledge, Urcuqui, 100650, Ecuador *camartinez@ffyb.uba.ar, both contributed equally to this work

Published
2015
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