Welcome to
Supramolecular Medicine !

RESEARCH

Our research focuses on the design, synthesis, and evaluation of supramolecular systems based on small molecules and peptides that operate under aqueous conditions. We employ different tools from organic chemistry, biophysics, and cell biology at different levels of complexity.

The final aim is to obtain a profound understanding of the relationship between molecular structure, morphology, and function in a biologically relevant environment.

Nowadays, our principal research is directed towards understanding the mechanism of peptide/protein self-assembly and its roles on the delicate balance between health and disease in gluten-related disorders. From our investigations, it is clear that gluten peptides are not only pathogenic for celiac patients. They possess interesting molecular and supramolecular features that could be used to disclose the mechanism of cellular uptake and be translated into other pathologies like aggregopathies and even cancer. This translational research is complemented with other more basic projects in the area of protein/peptide-protein interaction, and functional molecules like photoswitchable biosystems.

Gluten related-disorders and Protein-Protein Interaction

Gluten-related disorders are a group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. These disorders have a high prevalence in Western societies around 5% worldwide because gluten is present in wheat, rye, barley, and some varieties of oats.

It is accepted that the incomplete proteolysis of the gluten proteins is responsible for disease in susceptible individuals. From the chemical perspective, up to now, the research efforts focused on the identification, quantification, and separation of the components of gluten and connecting them with their pathological role in vitro and in vivo. Interestingly, while the primary structure of the molecules involved in the disease is known, there is a lack of information about their intrinsic behavior –such as their folding and molecular organization- under physiologically relevant conditions.

Gliadin and its 33-mer fragment have a central pathogenic role in the context of gluten-related. The aim of the present project is to elucidate the molecular, structural, and supramolecular basis of 33-mer oligomerization and the role of the 33-mer nanostructures in the delicate balance between health and disease.

Oligomerization and conformational transition, towards the β- parallel structure, are hallmarks of Alzheimer’s disease, Parkinson’s disease, and prion disease.

Based on these similarities, the relationship between 33-mer accumulations, due to proteolytical resistance, followed by oligomerization can be the up to now unknown trigger of disease before the onset of inflammation. This hypothesis opens new avenues to understand and treat this common pathology.

To prove this hypothesis, we moved from chemical and biophysics to immunological research, reporting for the first time that only large structures of 33-mer induce an innate immune response in macrophages which is mediated by Toll-like receptor (TLR) 4 activation. This result opens the understanding of the early stages of the disease. It connects activation of the innate immune system triggered by the presence of 33-mer protofilaments for the first time.

The current project combines different chemical and biological methodologies and approaches by including peptide chemistry, structural and supramolecular characterization methods, cellular biology approaches, proteomics, and super-resolution optical microscopy. By combining my research expertise and those of my collaborators, it will be possible to quantify and understand the role of the 33-mer oligomers as modulators of disease.

Our findings will open new avenues in the understanding of gluten-related disorders directed towards the design of new therapeutic targets beyond the gluten-free diet.

Funding: Deutsche Forschungsgemeinschaft (DFG)

Functional Molecules

Gluten-related disorders are a group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. These disorders have a high prevalence in Western societies around 5% worldwide because gluten is present in wheat, rye, barley, and some varieties of oats.

Remote Optocontrol of Biomembranes: In general, the use of azobenzene offers high quantum yield, minimal photo-bleaching, excellent photo-stability, and has the significant benefit of functional reversibility. However, it is the substantial conformation change in end-to-end distance of ~12 Å in the E state to a ~5– Å in the Z state that makes this system a practical one.

Recently, we reported a novel biomembrane photoswitch based on non-ionic azobenzene, C12OazoE3OH. There are other reports in the literature about the use of azobenzenes, but this report showed for the first time that a complex lipid membrane efficiently senses the molecular change of the azobenzene induced by light not only in bulk but also at interfaces, detecting changes in the membrane fluidity and organization.

Importantly, C12OazoE3OH might be used as a photoswitchable molecular probe in real systems, because it can penetrate a compact complex lipid membrane from the water subphase. Although it is useful for biophysical experiments, the implementation in living cells is diminished because of the use of UV-light.

L. A. Benedini, M. A. Sequeira, M. L. Fanani, B. Maggio, V. I. Dodero, J. Phys. Chem. B 120 (2016) 4053

Self-delivering systems: Directed self-assembly of functional small ℼ conjugated molecules offers unique opportunities to obtain discrete nanostructures of various sizes and shapes simply. Recently, self-delivering drugs with enhanced treatment efficacies in cancer have been described.

The driving forces are the strong intermolecular interactions such as hydrogen bonding, or ℼ-ℼ interactions. The presence of these interactions allows for the formation of stable, far-from-equilibrium nanostructures, which size and shape would depend on the molecular structure but also on the processing conditions.

Here, the directed self-assembly of drug/pro-drugs conjugates and other functional molecules with extended ℼ systems will be performed. The functional nanostructures will respond to an external stimulus as pH, ionic strength, redox properties and will be obtained easily by evaporation-induced self-assembly (EISA). Directed self-assembly not only offers an innovative way to craft self-delivering but also extends the use of molecular assembly as a toolbox to achieve functional nanostructures in water in the organic chemist’s Lab and to explore emerging properties of known approved supramolecular drugs.

Schematic EISA protocol. Adapted from M. A. Sequeira, M. G. Herrera, Z. B. Quirolo, V. I. Dodero, RSC Adv. 6 (2016) 108132

The final nano-container was used to deliver calcein, a water-soluble molecule, but it may also transport and deliver hydrophobic molecules during its E-Z photoisomerization.

The process consists of the controlled evaporation of the solvent under rotatory evaporation, allowing solute concentration and the formation of a thin organized mesostructure. Once the thin film is hydrated at the transition temperature, the formation of nano-objects in water might occur. This methodology is named evaporation-induced self-assembly (EISA) and is the easy way to obtain liposomes o polymersomes. However, to the best of our knowledge, this is the first time to be used successfully with a simple small azobenzene. Our findings open new opportunities to build up advanced materials in water using conjugated π systems in the organic chemistry Lab.

Peptide minimalistic self-assembly: Peptide structural transformation and aggregation is associated with a large number of outsider etiology diseases, and it is intrinsically linked to amyloid peptide aggregation. Diphenylalanine self-assembled structures are used as robust minimalist beta amyloids not only to elucidate protein aggregation but also to generate hydrogels and nanocarriers.

We employed a neutral model peptide Ac-Phe-Phe-Cys-NH2 (FFC) to elucidate the role of intermolecular disulfide bonds in protein fibrillation. The FFC peptide initially self-assembles into nanospheres that evolve to amyloid-type fibrils under mild oxidation conditions. On the other hand, incubation of the peptide in the presence of the chemical reduction agent, TCEP, inhibits the formation of the fibrils, detecting only spherical nanostructures with no secondary structure. Finally, we triggered the disintegration of the preformed amyloid fibrils by TCEP treatment. Under this condition, the amyloid bundles are transformed into rings, which evolve to a new spherical microstructure. We showed that the chemical reduction of intermolecular S-S in internal amyloid sequences might favor the off-path intermediates of amyloid fibril growth, even when the fibrils are formed.

Our findings demonstrated that in internal amyloid sequences, the thiol group might stabilize non-fibrillar structures, thus posing rational therapeutic strategies to control amyloid fibril formation associated with human diseases of unrelated origin.

The FFC supramolecular assembly depends on the encoded molecular information which is controlled by the oxide-reduction environment. From M. A. Sequeira, M. G. Herrera, V. I. Dodero Phys. Chem. Phys. , 2019, 21, 11916-11923.

Publications

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2022

(54) Wagh, Sandip K., Karen M. Lammers, Manohar V. Padul, Alfonso Rodriguez-Herrera, and Veronica I. Dodero. Celiac Disease and Possible Dietary Interventions: From Enzymes and Probiotics to Postbiotics and Viruses. Int. J. Mol. Sci, 2022, 23, no. 19: 11748. (REVIEW, IF: 5.924)

(53) M. G. Herrera, M. J. Amundarain, F. Nicoletti, M. Drechsler, M. Costabel, P. L. Gentili, V. I. Dodero, ChemBioChem 2022, e202200552. (ARTICLE, IF: 3.164)

(52) M. G. Herrera, M. Giampà, N. Tonali, V. I. Dodero. Multimodal methods to study protein aggregation and fibrillation, 77-102, in Advances in Protein Molecular and Structural Biology Methods, Academic Press, 2022 (BOOK CHAPTER).

(51) M. Giampà, M. J. Amundarain, M. G. Herrera, N. Tonali, V. I. Dodero. Implementing Complementary Approaches to Shape the Mechanism of α-Synuclein Oligomerization as a Model of Amyloid Aggregation, Molecules, 2022, 1, 88. (REVIEW, IF: 4,411).

2021

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(50) M. A. Lauxmann, D. S. Vazquez, H. M. Schilbert, P. R. Neubauer, K. M. Lammers, V. I. Dodero. From celiac disease to coccidia infection and vice-versa: The polyQ peptide CXCR3-interaction axis, BioEssays, 43 (12), 2100101 (HYPOTHESIS, IF: 4.345).

(49) M. G. Herrera, V. I. Dodero. Gliadin proteolytic resistant peptides: the interplay between structure and self-assembly in gluten-related disorders, Biophysical Reviews, 2021, 1-8. (REVIEW, IF 4.433).

(48) M.G. Herrera, F. Nicoletti, M. Gras, P. W. Dörfler, N. Tonali, Y. Hannappel, I. Ennen, A. Hütten, T. Hellweg, K. M. Lammers, V. I. Dodero. Pepsin Digest of Gliadin Forms Spontaneously Amyloid-Like Nanostructures Influencing the Expression of Selected Pro-Inflammatory, Chemoattractant, and Apoptotic Genes in Caco-2 Cells: Implications for Gluten-Related Disorders. Molecular nutrition & food research, 2021, 2100200. (ARTICLE, IF: 5.914, Journal Cover).

(47) N Tonali, L Hericks, DC Schröder, O Kracker, R Krzemieniecki, J Kaffy, V Le Joncour, P Laakkonen, A Marion, S Ongeri, V I Dodero, N Sewald. Peptidotriazolamers Inhibit Aβ (1-42) Oligomerization and Cross a Blood-Brain Barrier Model. ChemPlusChem, 2021, 86, 840-851. (ARTICLE, IF: 2.863).

(46) C. Schnepel, V. I. Dodero, N. Sewald. Novel Arylindigoids by Late-Stage Derivatization of Biocatalytically Synthesized Dibromoindigo. Chemistry – A European Journal, 2021, 27 (17), 5404. (ARTICLE, IF: 5.236).

(45) D. S. Vazquez, H. M. Schilbert, V. I. Dodero. Molecular and structural parallels between gluten pathogenic peptides and bacterial-derived proteins by bioinformatics analysis. Int. J. Mol. Sci, 2021, 22 (17), 9278. (ARTICLE, IF: 5.924)

2020

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(44) M. Florencia Pignataro, M. G. Herrera, V. I. Dodero. Evaluation of Peptide and Protein Self-Assembly by Spectroscopic Methods, Molecules, accepted (REVIEW, IF: 4.411).

(43) Ghabraie E, Kemker I, Tonali NM, Ismail M, Dodero VI, Sewald N. Phenothiazine-Biaryl Containing Fluorescent RGD Peptides Chemistry – A European Journal. , 2020,12036-12042. (ARTICLE, IF: 5.236)

(42) S. Müller, J. Paulus, J. Mattay, H. Ihmels, V. I. Dodero, N. Sewald. Photocontrolled DNA minor groove interactions of imidazole/pyrrole polyamides, Beilstein J. Org. Chem. 2020, 16, 60-70. doi:10.3762/bjoc.16 (ARTICLE, IF: 2.62).

2019

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(41) M. J. Amundarain, M. G. Herrera, F. Zamarreno, J. F. Viso, M. D. Costabel, V. I. Dodero. Molecular Mechanisms of 33-mer Gliadin Peptide Oligomerization, Phys. Chem. Phys. , 2019, 21, 22539. (ARTICLE, IF: 3.676).

(40) M. G. Herrera, M. F. Gómez Castro, E. Prieto, E. Barrera, V. I. Dodero, S. Pantano, F. Chirdo. Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease, 2019 FEBS Journal DOI: 10.1111/febs.15109. (ARTICLE, IF: 5.540).

(39) N. Tonali, V. I. Dodero, J. Kaffy, L. Hericks, S. Ongeri, N. Sewald. Real-time BODIPY-binding assay to screen inhibitors of the early oligomerization process of Aβ 1-42 peptide, 2019 ChemBioChem, DOI:10.1002/cbic.201900652 (ARTICLE, IF: 3.164).

(38) Z. B. Quirolo, M. Alejandra Sequeira, J. C. Martins, V. I. Dodero. Sequence-Specific DNA Binding by Noncovalent Peptide-Azocyclodextrin Dimer Complex as a Suitable Model for Conformational Fuzziness, Molecules 2019, 24 (13), 2508. (ARTICLE, IF: 4.411).

(37) M. A. Sequeira, M. G. Herrera, V. I. Dodero. Modulating amyloid fibrillation in a minimalist model peptide by intermolecular disulfide chemical reduction, Phys. Chem. Phys. , 2019, 21, 11916-11923. (ARTICLE, IF: 3.676).

2018

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(36) M. G. Herrera, M. Pizzuto. C. Lonez, K. Rott, A. Hütten, N. Sewald, J-M Ruysschaert, V. I. Dodero. Large Supramolecular Structures of 33-mer Gliadin Peptide Activate Toll-like Receptors in Macrophages, Nanomedicine: NBM 2018, 14, 1417-1427. (ARTICLE, IF: 5.91)

(35) M. G. Herrera, D. S Vazquez, R. Sreij, M, Dreschler, Y. Hertle, T. Hellweg, V. I. Dodero. Insights into gliadin oligomerization behavior at digestive pH 3.0, Colloids and Surfaces B: Biointerfaces, 2018, 165, 363-370. (ARTICLE, IF: 5.268).

(34) L. M. Lammers, M G. Herrera, V. I. Dodero. Translational chemistry meets gluten-related disorders, ChemistryOpen 2018, 7, 217 (Highlight in ChemistryViews 03/17/2018) (REVIEW, IF: 2.911).

(33) V. I. Dodero. Are gluten-related disorders a new protein aggregation disease? Proceedings of the 35th European Peptide Symposium, https://doi.org/10.17952/35EPS.2018.013 (PROCEEDING).

2016

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(32) M. A. Sequeira, M. G. Herrera, Z. B. Quirolo and V. I. Dodero. Easy Directed Assembly of a Nonionic Azoamphiphile Builds up Functional Azovesicles, RSC Adv., 2016, 6, 108132-108135. (ARTICLE, IF: 3.36).

(31) L. A. Benedini, M. Alejandra Sequeira, M. L. Fanani, B. Maggio, V. I. Dodero. Development of a Non-ionic Azobenzene Amphiphile for Remote Photocontrol of a Model Biomembrane, J. Phys. Chem. B, 2016, 120, 4053-4063. (ARTICLE, IF: 2.991).

(30) M. G. Herrera, T. V. Veuthey, V. I. Dodero. Self-organization of gliadin in aqueous media under physiological digestive pHs, Colloids and Surfaces B: Biointerfaces, 2016, 141, 565-575. (ARTICLE, IF: 5.268).

2015

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(29) M. G. Herrera, L. A. Benedini, C. Lonez, P. L. Schilardi, T. Hellweg, J.-M. Ruysschaert, VI. Dodero. Self-assembly of 33-mer gliadin peptide oligomers, Soft Matter, 2015, 11, 8648-8660. (ARTICLE, IF: 3.679).

2014

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(28) M. G. Herrera, F. Zamarreño, M. Costabel, H. Ritacco, A. Hütten, N. Sewald, V. I. Dodero. Circular Dichroism and Electron Microscopy Studies in vitro of 33-mer Gliadin Peptide Revealed Secondary Structure Transition and Supramolecular Organization, Biopolymers, 2014, 101, 96-106. (ARTICLE, IF: 2.505).

(27) Zulma Quirolo, L. Benedini, A. Sequeira, G. Herrera, T. Veuthey, V. I. Dodero. Understanding Recognition and Self-Assembly in Biology Using the Chemist’s Toolbox. Insight into Medicinal Chemistry, Current Topics in Medicinal Chemistry, 2014, 14, 730-739. (REVIEW, IF: 3.295).

(26) T. V. Veuthey, M. G. Herrera, V. I. Dodero. Dyes and stains: from molecular structure to histological application, Frontiers in Bioscience, Landmark Edition, 2014, 1, 91-112. (REVIEW, IF: 4.009).

(25) J. E. Colman Lerner, A. Morales, M. Aguilar, D. Giulani, M. Orte, J. Ditondo, V. I. Dodero, L. Massolo, E Y. Sánchez, N. Matamoros, A. Porta. The effect of air pollution on children’s health: a comparative study between La Plata and Bahía Blanca, Buenos Aires Province, Argentina, ENVIRONMENTAL IMPACT 2014, Vol 181, DOI: 10.2495/EID140561 (ARTICLE, IF: 4.549).

2013

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(24) Jiménez, V. I. Dodero, J. L. Mascareñas. Towards encoding reactivity using double stranded DNA. Sequence-dependent native chemical ligation of DNA binding polyamides,Tetrahedron, 2013, 69, 7847-7853. (ARTICLE, IF: 2.457).

(23) J. Mosquera, A. Jiménez-Balsa, V. I. Dodero, M. E. Vázquez, J. L. Mascareñas. Stimuli-responsive selection of target DNA sequences by synthetic bZIP peptides, Nat. Comm. , 2013, 4, 1874-1878. (ARTICLE, IF: 14.919).

(22) V. I. Dodero and P. V. Messina. Analyzing the Solution State of Protein Structure, Interactions, and Ligands by Spectroscopic Methods in Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science, 1-500, 2013, Ed. J. M. Ruso and A. Piñeiro, Wiley. ISBN: 978-1-1185-2317-9. (BOOK CHAP.)

(21) M. G. Herrera, V. I. Dodero. Self-assembly of Gliadin protein modulated by pH, Foods: Bioactives, Processing, Quality and Nutrition, 10-12 April 2013, Online Conference. X. (PROCEEDING.)

(20) M. A. Sequeira, V. I. Dodero. The Liquid Crystal Behavior of New Non-ionic Azobenzene-Amphiphiles, 16th International Electronic Conference on Synthetic Organic Chemistry, November 2012. editors: Julio A. Seijas, M. Pilar Vázquez-Tato, Shu-Kun Lin, CD-ROM, MDPI, Basel, Switzerland, 2013. ISBN 3-906980-26-X. (PROCEEDING.)

2011

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(19) V. I. Dodero, Z. B. Quirolo, M. A. Sequeira. Biomolecular studies by circular dichroism, Frontiers in Bioscience-Landmark Edition, 2011, 16, 61-73. (REVIEW, IF: 4.009).

(18) N. Hassan, P. V. Messina, V. I. Dodero, J. M. Ruso. Rheological properties of ovalbumin hydrogels as affected by surfactants addition, Int. J. Biol. Macromol. 2011, 48, 495-500. (ARTICLE, IF: 6.953).

2010

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(17) M. A. Sequeira, Z. B. Quirolo, V. I. Dodero. Synthesis and Characterization of Photomodulable amphiphiles, 14th Int. Electron. Conf. Synth. Org. Chem. 2010, A035:1-4. editor: Julio A. Seijas y M. Pilar Vázquez-Tato, CD-ROM edición, MDPI, Basel, Switzerland, 2010. ISBN 3-906980-24-3. PROCEEDING.

2007

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(16) P. V. Messina, G. Prieto, F. Salgado, C. Varela, M. Nogueira, V. I. Dodero, J. M. Ruso, F. Sarmiento. The Influence of Sodium Perfluorooctanoate on the Conformational Transitions of Human Immunoglobulin, Phys. Chem. B, 2007, 111, 8045 -8052. (ARTICLE, IF: 2.991).

(15) P. V. Messina, G. Prieto, J. Sabin, E. Blanco, C. Varela, V. I Dodero, J. M. Ruso, F. Sarmiento. A Potentiometric and Spectroscopic Study on the Interaction between Human Immunoglobulin G and Sodium Perfluorooctanoate in Aqueous Solution, Macromol. Symp. 2007, 251, 103 -111. (ARTICLE, IF: 0.85)

2006

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(14) J. B. Blanco, V. I. Dodero, M. E. Vázquez, M. Mosquera, L. Castedo, J. L. Mascareñas. Sequence-specific DNA binding by non-covalent peptide-tripyrrole conjugates, Angew. Chem. Int. ed., 2006, 118, 8390-8394. (ARTICLE, IF: 15,334).

(13) V. I. Dodero, M. Mosquera, J. B. Blanco, L. Castedo, J. L. Mascareñas. Modulating the Rate of a Native Ligation Coupling between Tripyrrole Derivatives by using Specific dsDNA, Organic Letters, 2006, 20 4433-4436. (ARTICLE, IF: 6.005).

(12) P. Messina, G. Prieto, V. I. Dodero, M. A. Cabrerizo-Vílchez, J. Maldonado-Valderrama, J. M. Ruso, P. Schulz, F. Sarmiento. Surface Characterization of Human Serum Albumin and Sodium Perfluorooctanoate Mixed Solutions by Pendant Drop Tensiometry and Circular Dichroism, Biopolymers, 2006, 82, 261-271. (ARTICLE, IF:2.505 )

(11) M. B. Faraoni, V. I. Dodero, L. C. Koll, A. E. Zúñiga, T. N. Mitchell, J. C. Podestá. Stereoselective hydrostannation of substituted alkynes initiated by triethyl boranes and reactivity of bulky triorganotin hydrides, Journal of Organometallic Chemistry, 2006, 691, 1085-1091. (ARTICLE, IF: 2.369).

2005

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(10) P. Messina, G. Prieto, V. I. Dodero, J. M. Ruso, P. Schulz, F. Sarmiento. Ultraviolet-Circular Dichroism Spectroscopy and Potentiometric Study of the Interaction between Human Serum Albumin and Sodium Perfluorooctanoate, Biopolymers, 2005, 5, 300-309. (ARTICLE, IF:2.505).

(9) V. I. Dodero, M. B. Faraóni, J. C. Podestá. Synthesis and some stereoselective radical additions of bis [(phenyldimethylsilyl) methyl] tin dihydride, Arkivoc, 2005, 12, 88-97. (ARTICLE, IF: 1.14)

(8) V. I. Dodero, M. B. Faraoni, D. C. Gerbino, L. C. Koll, A. E. Zúñiga, T. N. Mitchell, J. C. Podesta. Synthesis, Stereoselective Reactions, and Reactivity of 9-Triptycyldimethyltin Hydride, Organometallics, 2005, 24, 1992-1995. (ARTICLE, IF: 3.876).

2004

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(7) Darío Gerbino, B. Faraoni, V. I. Dodero, L. Koll, J. C. Podestá. Bulky organotin hydrides in palladium-catalyzed hydrostannation of terminal triple bonds, Editors: J. A. Seijas and M. P. Vázquez Tato, CD Edición sección A028, 2003. MDPI, Basel, Switzerland 2004. ISBN 3-906980-15-4. (PROCEEDING).

2003

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(6) V. I. Dodero, L. C. Koll, M. B. Faraoni, T. N. Mitchell, J. C. Podestá. Stereoselective Synthesis of Stannyl Enones via Palladium-Catalyzed and Free radical Hydrostannation of Alkynyl Ketones with Trineophyltin Hydride, Journal of Organic Chemistry, 2003, 68, 10087-10091. (ARTICLE, IF: 4.06).

(5) V. I. Dodero, N. N. Giagante, S. D. Mandolesi, A. Zúñiga, J. C. Podestá. Stereoselective addition of organotin anions to R-(+)-pulegone: a route to 8- triorganostannylmenthols, Arkivoc, X, 2003, 335-346. (ARTICLE, IF: 1.14).

(4) V. I. Dodero, T. N. Mitchell, J. C. Podestá. Synthesis and Free Radical Addition reaction of tris(phenyldimethylsilylmethyl)tin Hydride, Organometallics, 2003, 22, 856-860. (ARTICLE, IF: 3.876).

2002

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(3) V. I. Dodero, L. C. Koll, S. D. Mandolesi, J. C. Podestá. Stereoselective hydrostannation of substituted alkynes with trineophyltin hydride, Journal of Organometallic Chemistry, 2002, 650, 173-180. (ARTICLE, IF: 2.369).

2000

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(2) S. D. Mandolesi, N. N. Giagante, V. I. Dodero, J. C. Podestá. Stereoselective Synthesis of 8- trialkylstannylmenthols, Molecules, 5, 594-595, 2000. (COMM, IF: 4.411).

(1) V. I. Dodero, L.C. Koll, J. C. Podestá. Synthesis of Ethylenic and Acetylenic Triorganotin. with Bulky Organic Ligands, Molecules, 5, 439-440, 2000. MDPI, Basel Switzerland, ISBN 3-906980-15-4. (COMM, IF: 4.411).