Gerardo Corzo

UNAM Universidad Nacional Autónoma de México, Medicina Molecular y Bioprocesos, Faculty Member

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El Dr. Corzo es Ingeniero en Bioquímica Industrial por la Universidad Autónoma Metropolitana. Realizó una estancia de investigación sobre Biotecnología Marina en Tsukuba, Japón. Posteriormente, terminó sus estudios de Maestría en Biotecnología en el Instituto de Investigaciones Biomédicas de la UNAM. Consecutivamente, con el apoyo del programa Fullbright-García Robles, culminó sus estudios de doctorado en la Oklahoma State University. Posteriormente viajó a una estancia posdoctoral al “Suntory Institute for Bioorganic Research” en Osaka, Japón, donde al finalizar el periodo posdoctoral fue contratado como investigador asociado por cuatro años. En el 2004 se incorporó al Instituto de Biotecnología de la UNAM, donde actualmente es Investigador Titular “C” de tiempo completo en el Departamento de Medicina Molecular y Bioprocesos.

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Papers by Gerardo Corzo

Improved protease stability of the antimicrobial peptide Pin2 substituted with D-amino acids

by Elba Cristina Villegas Villarreal and Gerardo Corzo

Cationic antimicrobial peptides (AMPs) have attracted a great interest as novel class of antibiot... more Cationic antimicrobial peptides (AMPs) have attracted a great interest as novel class of antibiotics that might help in the treatment of infectious diseases caused by pathogenic bacteria. However, some AMPs with high antimicrobial activities are also highly hemolytic and subject to proteolytic degradation from human and bacterial proteases that limit their pharmaceutical uses. In this work a D-diastereomer of Pandinin 2, D-Pin2, was constructed to observe if it maintained antimicrobial activity in the same range as the parental one, but with the purpose of reducing its hemolytic activity to human erythrocytes and improving its ability to resist proteolytic cleavage. Although, the hydrophobic and secondary structure characteristics of Land D-Pin2 were to some extent similar, an important reduction in D-Pin2 hemolytic activity (30-40 %) was achieved compared to that of L-Pin2 over human erythrocytes. Furthermore, D-Pin2 had an antimicrobial activity with a MIC value of 12.5 lM towards Staphylococcus aureus, Escherichia coli, Streptococcus agalactiae and two strains of Pseudomonas aeruginosa in agar diffusion assays, but it was half less potent than that of L-Pin2. Nevertheless, the antimicrobial activity of D-Pin2 was equally effective as that of L-Pin2 in microdilution assays. Yet, when D-and L-Pin2 were incubated with trypsin, elastase and whole human serum, only D-Pin2 kept its antimicrobial activity towards all bacteria, but in diluted human serum, Land D-Pin2 maintained similar peptide stability. Finally, when Land D-Pin2 were incubated with proteases from P. aeruginosa DFU3 culture, a clinical isolated strain, D-Pin2 kept its antibiotic activity while L-Pin2 was not effective. Keywords D-diastereomer Á Peptide Á Antimicrobial Á Hemolysis Á Enzyme degradation Abbreviations RP-HPLC Reverse-phase HPLC HPLC High pressure liquid chromatography MHB Mueller-Hinton broth MHA Mueller-Hinton agar CFU Colony forming units CD Circular dichroism AMP Cationic antimicrobial peptide MIC Minimal inhibitory concentrations TFA Trifluoroacetic acid PBS Phosphate buffer saline, pH 7.2 PAGE Polyacrylamide gel electrophoresis SDS Sodium dodecyl sulfate TFE 2,2,2-trifluoroethanol Electronic supplementary material The online version of this article (

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The arachnids poisons: their outstanding insecticide strength and their unusual antibiotic capacity

Tema del mesDentro de los diferentes órdenes que comprenden al grupo de los arácnidos, el orden a... more Tema del mesDentro de los diferentes órdenes que comprenden al grupo de los arácnidos, el orden aranae (arañas y tarántulas) y el orden scorpiones (alacranes) son de particular interés científico debido a que agrupan animales capaces de producir venenos. El desarrollo de la producción de venenos les confiere la capacidad de defenderse de sus depredadores y a la vez son una herramienta indispensable para la captura de sus presas. El veneno de alacranes y arañas es una mezcla compleja de diferentes componentes químicos y proteicos, dentro de los que destacan mayormente las toxinas que afectan canales iónicos y en poca medida, pero de importancia significativa, los péptidos antibióticos. Se ha demostrado que dentro de la diversidad de toxinas provenientes del veneno de estos animales, existen algunas con actividad exclusiva sobre canales de insecto, por tal motivo han sido propuestas como una alternativa para el control biológico de insectos plaga en agricultura y de insectos vectores ...

Bile Salt Deconjugation by Three Strains of Lactobacillus Acidophilus and Characterization of Their Bile Salt Hydrolase

11 Bile salt hydrolase activity in spent broth after cell growth in MRS broth supplemented with 2... more

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Design of short alpha-helical peptides and their activity against pathogenic bacteria Mycobacterium tuberculosis

The contention of multidrug-resistant bacteria requires the use of new antibiotics. Pandinin 2 (P... more The contention of multidrug-resistant bacteria requires the use of new antibiotics. Pandinin 2 (Pin2) is a highly hemolytic antimicrobial peptide that has a central proline residue. Proline forms a structural ‘‘kink’’ linked to its pore-forming activity towards human erythrocytes. In this work, the residue Pro14 of Pin2 was both substituted and flanked by Glycine residues according to the low hemolytic activities of antimicrobial peptides as Magainins and Ponericins, respectively. Both Pin2 variants showed antimicrobial activity against E. coli, S. aureus, and M. tuberculosis. However, Pin2 [GPG] was 30% less hemolytic. To avoid the drawback associated to the cost of synthesis of large peptides, two short peptides were designed and synthesized based on Pin2 [G] and Pin2 [GPG]. Both Pin2 [14] and Pin2 [17] short variants, showed antibiotic activities against E. coli and M. tuberculosis. Besides, Pin2 [14] presented only 25% of hemolysis at 100 μM, while the peptide Pin2 [17] did not ...

An overview of some enzymes from buthid scorpion venoms from Colombia: Centruroides margaritatus, Tityus pachyurus, and Tityus n. sp. aff. metuendus

The Journal of venomous animals and toxins including tropical diseases, 2024

Background: In Colombia, several species of Buthidae scorpions belonging to the genera Centruroid... more Background: In Colombia, several species of Buthidae scorpions belonging to the genera Centruroides and Tityus coexist, and their stings are considered life-threatening to humans because of their venom neurotoxins. Despite previous studies focusing on neurotoxins from these scorpion genera, little is known about the enzymes present in their venoms and their relationship with whole venom toxicity. Methods: Here, using proteomic and biochemical protocols the enzymatic activities of the venoms of three Colombian scorpion species, C. margaritatus, T. pachyurus, and T. n. sp. aff. metuendus, were compared to establish the presence and absence of enzymes such as phospholipases, hyaluronidases, and proteases that could be related to venom toxicity. Results: C. margaritatus was positive for hyaluronidases, T. n. sp. aff. metuendus for proteases, and T. pachyurus exhibited activity for all three mentioned enzymes. Conclusion: This information provides valuable insights into the specific enzyme diversity of each species' venom and their potential role in venom toxicity, which could contribute to the development of better treatments and prevention strategies for scorpion envenomation.

format_quoteOnly fraction 80 of C. margaritatus venom exhibited hyaluronidase activity, revealing unique enzymatic characteristics within the species.format_quote

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Heterologous expression of four recombinant toxins from Panamanian scorpions of the genus Tityus and Centruroides for production of antivenom

Toxicon: X, Mar 1, 2022

Background The development of more effective antivenoms remains a necessity for countries where s... more Background The development of more effective antivenoms remains a necessity for countries where scorpionism is a public health problem. Also, the regionalization of antivenoms may be important for some countries with special scorpionism characteristics. Objective Production of antibodies capable of neutralizing the lethal effect of the venom of three scorpion species from Panama. Methods The primary structures of two neurotoxins from T. pachyurus, one from T. cerroazul and another from C. bicolor were elucidated using N-terminal amino acid degradation and Sanger gene cloned sequencing. The obtained mRNA transcripts were cloned and expressed using E. coli vectors. Different bacterial expression conditions were tested and the best culture conditions for each expressed protein is reported. The expressed scorpion toxins were purified by chromatographic methods and used as immunogens in rabbits. Results The antibodies produced under the reported immunization scheme show better neutralization (ED50) than other reported commercial antivenoms used to neutralize similar species scorpion venoms under similar LD50 conditions. Conclusion The information reported here shows the proof of concept for selecting recombinant immunogens with the ability to produce antibodies for neutralizing the lethal effects of the most important medical species of scorpions in Panama.

Use of irradiated elapid and viperid venoms for antivenom production in small and large animals

Toxicon, Dec 1, 2018

This work evaluated the feasibility of using toxoids obtained by gamma radiation in the productio... more This work evaluated the feasibility of using toxoids obtained by gamma radiation in the production of antivenoms in small and large animals. Mixtures of African snake venoms from viperids or elapids were used. The viperid mixture contained the crude venom of five species of the genera Echis and Bitis, while the elapid mixture contained the crude venom of six species of the genera Naja and Dendroaspis. The viperid mixture had an LD 50 of 1.25 mg/kg in mice, and the elapid mixture had an LD 50 of 0.46 mg/kg. Both viper and elapid aqueous mixtures were subjected to Cobalt-60 gamma irradiation in three physical states: lyophilized, frozen and liquid. Radiation doses ranged from 0.5 to 100 kGy. The LD 50 s of the lyophilized and frozen mixtures of both viperid and elapid mixtures remained unaltered with radiation doses as high as 100 kGy; nevertheless, in the liquid state, doses of 3.5 and 5.5 kGy reduced the venom toxicity of both the viperid and elapid mixtures to 7.25 mg/kg and 1.74 mg/kg; less toxic by factors of 5.8 and 3.8, respectively. Groups of four rabbits and three horses were immunized with either irradiated or non-irradiated mixtures. In vitro and in vivo analysis of the rabbit and horse sera revealed that neutralizing antibodies were produced against both irradiated (toxoids) and native venom mixtures. None of the animals used in this study, either immunized with native venom or toxoids, developed severe local effects due to the application of venoms mixtures. Gammairradiated detoxified venoms mixtures, under well-controlled and studied conditions, could be a practical alternative for the production of polyvalent equine serum with high neutralization potency against snake venoms.

Reptilian β-defensins: Expanding the repertoire of known crocodylian peptides

Peptides, Feb 1, 2021

One of the major families of host defense peptides (HDPs) in vertebrates are β-defensins. They co... more One of the major families of host defense peptides (HDPs) in vertebrates are β-defensins. They constitute important components of innate immunity and have remained an interesting topic of research for more than two decades. While many β-defensin sequences in mammals and birds have been identified and their properties and functions characterized, β-defensin peptides from other groups of vertebrates, particularly reptiles, are still largely unexplored. In this review, we focus on reptilian β-defensins and summarize different aspects of their biology, such as their genomic organization, evolution, structure, and biological activities. Reptilian β-defensin genes exhibit similar genomic organization to birds and their number and gene structure are variable among different species. During the evolution of reptiles, several gene duplication and deletion events have occurred and the functional diversification of β-defensins has been mainly driven by positive selection. These peptides display broad antimicrobial activity in vitro, but a deeper understanding of their mechanisms of action in vivo, including their role as immunomodulators, is still lacking. Reptilian β-defensins constitute unique polypeptide sequences to expand our current understanding of innate immunity in these animals and elucidate core biological functions of this family of HDPs across amniotes.

Discovery of human Hv1 channel peptide inhibitors

Biophysical Journal, 2022

Identification, chemical synthesis and heterologous expression of an antinociceptive peptide from the veined tree frog Trachycephalus typhonius

Process Biochemistry, 2017

 A peptide named Tt7 was secreted from the skin of an American frog, and it was able to elicit a... more  A peptide named Tt7 was secreted from the skin of an American frog, and it was able to elicit analgesic activity in mice.  The peptide Tt7 contains similar primary structure to an Asian frog, a prove of survival of the fittest molecule.  The heterologous expressed peptide HisrTt7 and the native one have similar secondary structure and analgesic activity.  The analgesic peptide has low activity on Nav1.7 and on the acid gated currents.

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Transcriptomic comparison of the royal jelly proteins coded in the hypopharyngeal glands of Apis mellifera and Geotrigona acapulconis

Research Square (Research Square), Jul 12, 2023

Apis mellifera and Geotrigona acapulconis are two members of Apidae family with large morphologic... more Apis mellifera and Geotrigona acapulconis are two members of Apidae family with large morphological differences; that is G. acapulconis is stingless, smaller in size, lack of yellow pigmentation, different nest building and hive structure, among other differences. We also suggest that there are biochemical differences between A. mellifera and G. acapulconis related to the composition of their Royal Jelly proteins (RJPs) and Yellow family proteins (YFPs). For instances, it has been reported that RJPs are involved in larval development of A. mellifera, and the YFPs play an important role in pigmentation in these arthropods. In this work, the protein composition of RJPs and YFPs were investigated indirectly by performing transcriptome analysis of the hypopharyngeal glands (HG), which are the RJP and YFPs producers. The results showed the presence of transcripts coding for RJPs in both bees. These proteins belonging to the Major Royal Jelly proteins (MRJPs) only recorded in A. mellifera and YFPs, which were identi ed here in both bees, but in different proportions. Additionally, MRJPs were only found in A. mellifera. Yet, coding sequences of these type proteins were found as Royal Jelly protein-like (RJPL) in G. acalpuconis, which are evolved from the MRJP. Furthermore, the differences found between yellow proteins (YPs) could be directly associated to the color of such bees, and the lack of MRJPs in G. acapulconis, that are important for larval nutrition and development, could be a consequence of a poor development of the larvae. On the other hand, some of the differences could be the result of their different behavior. Some MRJPs are required for defense of the larvae against pathogens, which are related to the differences in their biological cycle. Unfortunately, other functions of RJPs are not yet fully characterized; so, it is imperative to continue the research of the functions of RJPs in bees for a better understanding of their biological role.

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Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and high-performance liquid chromatography study of quantitative and qualitative variation in tarantula spider venoms

Rapid Communications in Mass Spectrometry, Jan 25, 2002

Animal venoms are important sources of novel pharmacological tools, useful in biochemical charact... more Animal venoms are important sources of novel pharmacological tools, useful in biochemical characterization of their receptors. Venom quality control, batch-to-batch homogeneity and high reproducibility of venom fractionation and toxin purification are crucial issues for biochemical and pharmacological studies. To address these issues, a study of the variability of tarantula spider venom samples was undertaken. Venom profiles of samples collected from individuals of different age and sex, and from sibling spiders of the same species, were generated by high-performance liquid chromatography (HPLC) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and analyzed to assess venom variability and method accuracy. Sex-linked venom variation was studied on eight species. Clear qualitative differences were observed for six out of eight species, as well as quantitative differences. Age-related variation studied in Poecilotheria rufilata showed essentially age-related quantitative differences between adults of both sexes and immature juveniles. The venoms of nine siblings and three wild-collected Pterinochilus murinus were studied for individual variation, showing only very minor quantitative differences. On the same samples, the quality of MALDI-TOFMS venom fingerprinting was demonstrated to be highly reproducible. Our results show that tarantula venom peptide fingerprinting is a highly reliable identification method, that pooled batches of venom from several animals can be used for venom purification, that venom composition does not appear to be qualitatively related to ontogenesis in the spiders studied, and that qualitative sex-linked variation occurs across most species and may be important in activity studies.

Review Pharmacologically active spider peptide toxins

Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophys- ... more Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophys- iology have permitted the isolation and identification of numerous novel peptide toxins from animal venoms in re- cent years. These advances have also opened up the field of spider venom research, previously unexplored due to methodological limitations. Many peptide toxins from spider venoms share structural features, amino acid com- position and consensus sequences that allow them to in- teract with related classes of cellular receptors. They have become increasingly useful agents for the study of volt- age-sensitive and ligand-gated ion channels and the dis-

Recombinant expression of leptin hormone in <em>Pichia pastoris</em>, as a biosimilar option for orphan disease treatment

Proceedings of 7th International Electronic Conference on Medicinal Chemistry, Nov 3, 2021

Identification of a crocodylian β-defensin variant from Alligator mississippiensis with antimicrobial and antibiofilm activity

Peptides, Jul 1, 2021

β-defensin host defense peptides are important components of the innate immune system of vertebra... more β-defensin host defense peptides are important components of the innate immune system of vertebrates. Although evidence of their broad antimicrobial, antibiofilm and immunomodulatory activities in mammals have been presented, β-defensins from other vertebrate species, like crocodylians, remain largely unexplored. In this study, five new crocodylian β-defensin variants from Alligator mississippiensis and Crocodylus porosus were selected for synthesis and characterization based on their charge and hydrophobicity values. Linear peptides were synthesized, folded, purified and then evaluated for their antimicrobial and antibiofilm activities against the bacterial pathogens, Salmonella enterica serovar Typhimurium, Staphylococcus aureus, Enterobacter cloacae and Acinetobacter baumannii. The Am23SK variant (SCRFSGGYCIWNWERCRSGHFLVALCPFRKRCCK) from A. mississippiensis displayed promising activity against both planktonic cells and bacterial biofilms, outperforming the human β-defensin 3 under the experimental conditions. Moreover, Am23SK exhibited no cytotoxicity towards mammalian cells and exerted immunomodulatory effects in vitro, moderately suppressing the production of proinflammatory mediators from stimulated human bronchial epithelial cells. Overall, our results have expanded the activity landscape of crocodylian and reptilian β-defensin in general.