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Archer, M., AL Carvalho, S. Teixeira, I. Moura, JJG Moura, F. Rusnak, and MJ Romao. "Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein." Protein Science. 8 (1999): 1536-1545. Abstract
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Branco, Paula S., Daniela Peixoto, Margarida Figueiredo, Gabriela Malta, Catarina Roma-Rodrigues, Pedro Viana Batista, Alexandra R. Fernandes, Sónia Barroso, Ana Luisa Carvalho, Carlos A. M. Afonso, and Luísa Maria Ferreira. "Synthesis, cytotoxicity evaluation in human cell lines and in vitro DNA interaction of a hetero arylidene-9(10H)-anthrone." European Journal of Organic Chemistry (2018): n/a–n/a. AbstractWebsite

A new and never yet reported hetero arylidene-9(10H)-anthrone structure (4) was unexpectedly isolated on reaction of 1,2-dimethyl-3-ethylimidazolium iodide (2) and 9-anthracenecarboxaldehyde (3) under basic conditions. Its structure was unequivocally attributed by X-ray crystallography. No cytotoxicity in human healthy fibroblasts and in two different cancer cell lines was observed indicating its applicability in biological systems. Compound 4 interacts with CT-DNA by intercalation between the adjacent base pairs of DNA with a high binding affinity (Kb = 2.0(± 0.20) x 105 M-1) which is 10x higher than that described for doxorubicin (Kb = 3.2 (±0.23) × 104 M-1). Furthermore, compound 4 quenches the fluorescence emission of GelRed-CT-DNA system with a quenching constant (KSV) of 3.3(±0.3) x 103 M-1 calculated by the Stern-Volmer equation.

Brás, Joana L. A., Benedita A. Pinheiro, Kate Cameron, Fiona Cuskin, Aldino Viegas, Shabir Najmudin, Pedro Bule, Virginia M. R. Pires, Maria João Romão, Edward A. Bayer, Holly L. Spencer, Steven Smith, Harry J. Gilbert, Victor D. Alves, Ana Luísa Carvalho, and Carlos M. G. A. Fontes. "Diverse specificity of cellulosome attachment to the bacterial cell surface." Scientific Reports. 6 (2016): 38292. AbstractWebsite

During the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.

Bras, Joana L. A., Victor D. Alves, Ana Luisa Carvalho, Shabir Najmudin, Jose A. M. Prates, Luis M. A. Ferreira, David N. Bolam, Maria Joao Romao, Harry J. Gilbert, and Carlos M. G. A. Fontes. "Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode." The Journal of biological chemistry. 287 (2012): 44394-405.Website
Bras, Joana L. A., Alan Cartmell, Ana Lusia M. Carvalho, Genny Verze, Edward A. Bayer, Yael Vazana, Marcia A. S. Correia, Jose A. M. Prates, Supriya Ratnaparkhe, Alisdair B. Boraston, Maria J. Romao, Carlos M. G. A. Fontes, and Harry J. Gilbert. "Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis (vol 108, pg 5237, 2011)." Proceedings of the National Academy of Sciences of the United States of America. 108 (2011): 8525. Abstract
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Bras, Joana L. A., Ana Luisa Carvalho, Aldino Viegas, Shabir Najmudin, Victor D. Alves, Jose A. M. Prates, Luis M. A. Ferreira, Maria J. Romao, Harry J. Gilbert, and Carlos M. G. A. Fontes. "Escherichia coli expression, purification, crystallization, and structure determination of bacterial cohesin-dockerin complexes." Methods in enzymology. Vol. 510. 2012. 395-415. Abstract

Cellulosomes are highly efficient nanomachines that play a fundamental role during the anaerobic deconstruction of complex plant cell wall carbohydrates. The assembly of these complex nanomachines results from the very tight binding of repetitive cohesin modules, located in a noncatalytic molecular scaffold, and dockerin domains located at the C-terminus of the enzyme components of the cellulosome. The number of enzymes found in a cellulosome varies but may reach more than 100 catalytic subunits if cellulosomes are further organized in polycellulosomes, through a second type of cohesin-dockerin interaction. Structural studies have revealed how the cohesin-dockerin interaction mediates cellulosome assembly and cell-surface attachment, while retaining the flexibility required to potentiate catalytic synergy within the complex. Methods that might be applied for the production, purification, and structure determination of cohesin-dockerin complexes are described here. Copyright 2012 Elsevier Inc. All rights reserved.

Bule, Pedro, Victor D. Alves, Vered Israeli-Ruimy, Ana L. Carvalho, Luís M. A. Ferreira, Steven P. Smith, Harry J. Gilbert, Shabir Najmudin, Edward A. Bayer, and Carlos M. G. A. Fontes. "Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes." Scientific Reports. 7.1 (2017): 759. AbstractWebsite

Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens’ cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.

Bule, Pedro, Virgínia M. R. Pires, Victor D. Alves, Ana Luísa Carvalho, José A. M. Prates, Luís M. A. Ferreira, Steven P. Smith, Harry J. Gilbert, Ilit Noach, Edward A. Bayer, Shabir Najmudin, and Carlos M. G. A. Fontes. "Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction." Scientific Reports. 8.1 (2018): 6987. AbstractWebsite

Cellulosomes are highly sophisticated molecular nanomachines that participate in the deconstruction of complex polysaccharides, notably cellulose and hemicellulose. Cellulosomal assembly is orchestrated by the interaction of enzyme-borne dockerin (Doc) modules to tandem cohesin (Coh) modules of a non-catalytic primary scaffoldin. In some cases, as exemplified by the cellulosome of the major cellulolytic ruminal bacterium Ruminococcus flavefaciens, primary scaffoldins bind to adaptor scaffoldins that further interact with the cell surface via anchoring scaffoldins, thereby increasing cellulosome complexity. Here we elucidate the structure of the unique Doc of R. flavefaciens FD-1 primary scaffoldin ScaA, bound to Coh 5 of the adaptor scaffoldin ScaB. The RfCohScaB5-DocScaA complex has an elliptical architecture similar to previously described complexes from a variety of ecological niches. ScaA Doc presents a single-binding mode, analogous to that described for the other two Coh-Doc specificities required for cellulosome assembly in R. flavefaciens. The exclusive reliance on a single-mode of Coh recognition contrasts with the majority of cellulosomes from other bacterial species described to date, where Docs contain two similar Coh-binding interfaces promoting a dual-binding mode. The discrete Coh-Doc interactions observed in ruminal cellulosomes suggest an adaptation to the exquisite properties of the rumen environment.

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Carvalho, AL, L. Sanz, D. Barettino, A. Romero, JJ Calvete, and MJ Romao. "Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: A homologue of human PSA." Journal of Molecular Biology. 322 (2002): 325-337. Abstract
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Carvalho, AL, FMV Dias, JAM Prates, T. Nagy, HJ Gilbert, GJ Davies, LMA Ferreira, MJ Romao, and CMGA Fontes. "Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex." Proceedings of the National Academy of Sciences of the United States of America. 100 (2003): 13809-13814. Abstract
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Carvalho, Ana Luisa, Fernando M. V. Dias, Tibor Nagy, Jose A. M. Prates, Mark R. Proctor, Nicola Smith, Edward A. Bayer, Gideon J. Davies, Luis M. A. Ferreira, Maria J. Romao, Carlos M. G. A. Fontes, and Harry J. Gilbert. "Evidence for a dual binding mode of dockerin modules to cohesins." Proceedings of the National Academy of Sciences of the United States of America. 104 (2007): 3089-3094. Abstract
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Carvalho, AL, A. Goyal, JAM Prates, DN Bolam, HJ Gilbert, VMR Pires, LMA Ferreira, A. Planas, MJ Romao, and CMGA Fontes. "The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site." Journal of Biological Chemistry. 279 (2004): 34785-34793. Abstract
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Carvalho, Ana Luísa, José Trincão, and Maria João Romão. "X-Ray Crystallography in Drug Discovery." Methods in molecular biology (Clifton, N.J.). Vol. 572. 2010. 31-56. Abstract

Macromolecular X-ray crystallography is an important and powerful technique in drug discovery, used by pharmaceutical companies in the discovery process of new medicines. The detailed analysis of crystal structures of protein-ligand complexes allows the study of the specific interactions of a particular drug with its protein target at the atomic level. It is used to design and improve drugs. The starting point of these studies is the preparation of suitable crystals of complexes with potential ligands, which can be achieved by using different strategies described in this chapter. In addition, an introduction to X-ray crystallography is given, highlighting the fundamental steps necessary to determine the three-dimensional structure of protein-ligand complexes, as well as some of the tools and criteria to validate crystal structures available in databases.

Carvalho, Ana Luísa, Teresa Santos-Silva, Maria João Romão, J. Eurico, and Filipa Marcelo. "{CHAPTER 2 Structural Elucidation of Macromolecules}." Essential Techniques for Medical and Life Scientists: A Guide to Contemporary Methods and Current Applications with the Protocols. BENTHAM SCIENCE PUBLISHERS, 2018. 30-91. Abstract

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Carvalho, AL, VMR Pires, TM Gloster, JP Turkenburg, JAM Prates, LMA Ferreira, MJ Romao, GJ Davies, CMGA Fontes, and HJ Gilbert. "Insights into the structural determinants of cohesin dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA." Journal of Molecular Biology. 349 (2005): 909-915. Abstract
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Carvalho, AL, JM Dias, L. Sanz, A. Romero, JJ Calvete, and MJ Romao. "Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma." Acta Crystallographica Section D-Biological Crystallography. 57 (2001): 1180-1183. Abstract

The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purired from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 Angstrom resolution were collected at the ESRF synchrotron-radiation source.

Caseiro, Catarina, Nicholas G. S. McGregor, Victor Diogo Alves, Ana Luísa Carvalho, Maria João Romão, Gideon J. Davies, Carlos M. G. A. Fontes, and Pedro Bule. "Family GH157 enzyme exhibits broad linkage tolerance and a dual endo/exo- β -glucanase activity on β-glucans." (2024): 137402. AbstractWebsite

The structural and chemical diversity of β-glucans is reflected on the variety of essential biological roles tackled by these polysaccharides. This natural heterogeneity requires an elaborate assortment of enzymatic mechanisms to assemble, degrade or modify, as well as to extract their full biotechnological potential. Recent metagenomic efforts have provided an unprecedented growth in potential new biocatalysts, most of which remain unconfirmed or uncharacterized. Here we report the first biochemical and structural characterization of two bacterial β-glucanases from the recently created glycoside hydrolase family 157 (LaGH157 and BcGH157) and investigate their molecular basis for substrate hydrolysis. Structural analysis by X-ray crystallography revealed that GH157 enzymes belong to clan GH-A, possessing a (β/α)8-barrel fold catalytic domain, two β-sandwich accessory domains and two conserved catalytic glutamates residues, with relative positions compatible with a retaining mechanism of hydrolysis. Specificity screening and enzyme kinetics suggest that the enzymes prefer mixed-linkage glucans over β-1,3-glucans. Activity screening showed that both enzymes exhibit pH optimum at 6.5 and temperature optimum for LaGH157 and BcGH157 at 25 °C and 48 °C, respectively. Product analysis with HPAEC-PAD and LC-MS revealed that both enzymes are endo-1,3(4)-β-glucanases, capable of cleaving β-1,3 and β-1,4-linked glucoses, when preceded by a β-1,3 linkage. Moreover, BcGH157 needs a minimum of 4 subsites occupied for hydrolysis to occur, while LaGH157 only requires 3 subsites. Additionally, LaGH157 possesses exohydrolytic activity on β-1,3 and branching β-1,6 linkages. This unusual bifunctional endo-1,3(4)/exo-1,3–1,6 activity constitutes an expansion on our understanding of β-glucan deconstruction, with the potential to inspire future applications.

Coelho, Catarina, Pablo J. Gonzalez, Jose Trincao, Ana L. Carvalho, Shabir Najmudin, Thomas Hettman, Stephan Dieckman, Jose J. G. Moura, Isabel Moura, and Maria J. Romao. "Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis." Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 63 (2007): 516-519. Abstract
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Correia, Viviana G., Benedita A. Pinheiro, Ana Luísa Carvalho, and Angelina S. Palma. "Resistance to Aminoglycosides." Antibiotic Drug Resistance. John Wiley & Sons, Ltd, 2019. 1-38. Abstract

Summary The emergence of bacterial resistance to different antibiotics in clinical use, together with the knowledge on the mechanisms by which bacteria resist the action of aminoglycosides, have contributed to the renewed interest in these molecules as potential antimicrobials. Here, we give an overview on natural and semisynthetic aminoglycosides and their structural features and modes of action, focusing on the structural insight underlying resistance mechanisms. Developments on carbohydrate chemistry and microarray technology are highlighted as powerful approaches toward generation of new aminoglycosides and for screening their interactions with RNAs and proteins. The link between antibiotic uptake and the human gut microbiome is also addressed, focusing on gut microbiome function and composition, antibiotic-induced alterations in host health, and antibiotic resistance. In addition, strategies to modulate human microbiome responses to antibiotics are discussed as novel approaches for aminoglycoside usage and for the effectiveness of antibiotic therapy.

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Dias, JM, AL Carvalho, I. Kolln, JJ Calvete, E. TopferPetersen, P. F. Varela, A. Romero, C. Urbanke, and MJ Romao. "Crystallization and preliminary x-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture." Protein Science. 6 (1997): 725-727. Abstract

{Bovine acidic seminal fluid protein (aSFP) is a 12.9 kDa polypeptide of the spermadhesin family built by a single CUB domain architecture. The CUB domain is an extracellular module present in 16 functionally diverse proteins. To determine the three-dimensional structure of aSFP, the protein was crystallized at 21 degrees C by vapor diffusion in hanging drops, using ammonium sulfate, pH 4.7, and polyethyleneglycol 4000 as precipitants, containing 10% dioxane to avoid the formation of clustered crystals. Elongated prismatic crystals with maximal size of 0.6 x 0.3 x 0.2 mm(3) diffract to beyond 1.9 Angstrom resolution and belong to space group P2(1)2(1)2, with cell parameters a = 52.4 Angstrom

Dias, Ana Margarida Gonçalves Carvalho, Inês Pimentel Moreira, Iana Lychko, Cátia Lopes Soares, Arianna Nurrito, Arménio Jorge Moura Barbosa, Viviane Lutz-Bueno, Raffaele Mezzenga, Ana Luísa Carvalho, Ana Sofia Pina, and Ana Cecília Afonso Roque. "Hierarchical self-assembly of a reflectin-derived peptide." Frontiers in Chemistry. 11 (2023). AbstractWebsite

Reflectins are a family of intrinsically disordered proteins involved in cephalopod camouflage, making them an interesting source for bioinspired optical materials. Understanding reflectin assembly into higher-order structures by standard biophysical methods enables the rational design of new materials, but it is difficult due to their low solubility. To address this challenge, we aim to understand the molecular self-assembly mechanism of reflectin’s basic unit—the protopeptide sequence YMDMSGYQ—as a means to understand reflectin’s assembly phenomena. Protopeptide self-assembly was triggered by different environmental cues, yielding supramolecular hydrogels, and characterized by experimental and theoretical methods. Protopeptide films were also prepared to assess optical properties. Our results support the hypothesis for the protopeptide aggregation model at an atomistic level, led by hydrophilic and hydrophobic interactions mediated by tyrosine residues. Protopeptide-derived films were optically active, presenting diffuse reflectance in the visible region of the light spectrum. Hence, these results contribute to a better understanding of the protopeptide structural assembly, crucial for the design of peptide- and reflectin-based functional materials.

Duarte, Marlene, Victor D. Alves, Márcia Correia, Catarina Caseiro, Luís M. A. Ferreira, Maria João Romão, Ana Luísa Carvalho, Shabir Najmudin, Edward A. Bayer, Carlos M. G. A. Fontes, and Pedro Bule. "Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein assemblies." International Journal of Biological Macromolecules. 224 (2023): 55-67. AbstractWebsite

The cellulosome is an elaborate multi-enzyme structure secreted by many anaerobic microorganisms for the efficient degradation of lignocellulosic substrates. It is composed of multiple catalytic and non-catalytic components that are assembled through high-affinity protein-protein interactions between the enzyme-borne dockerin (Doc) modules and the repeated cohesin (Coh) modules present in primary scaffoldins. In some cellulosomes, primary scaffoldins can interact with adaptor and cell-anchoring scaffoldins to create structures of increasing complexity. The cellulosomal system of the ruminal bacterium, Ruminococcus flavefaciens, is one of the most intricate described to date. An unprecedent number of different Doc specificities results in an elaborate architecture, assembled exclusively through single-binding-mode type-III Coh-Doc interactions. However, a set of type-III Docs exhibits certain features associated with the classic dual-binding mode Coh-Doc interaction. Here, the structure of the adaptor scaffoldin-borne ScaH Doc in complex with the Coh from anchoring scaffoldin ScaE is described. This complex, unlike previously described type-III interactions in R. flavefaciens, was found to interact in a dual-binding mode. The key residues determining Coh recognition were also identified. This information was used to perform structure-informed protein engineering to change the electrostatic profile of the binding surface and to improve the affinity between the two modules. The results show that the nature of the residues in the ligand-binding surface plays a major role in Coh recognition and that Coh-Doc affinity can be manipulated through rational design, a key feature for the creation of designer cellulosomes or other affinity-based technologies using tailored Coh-Doc interactions.

Duarte, Marlene, Aldino Viegas, Victor D. Alves, José A. M. Prates, Luís M. A. Ferreira, Shabir Najmudin, Eurico J. Cabrita, Ana Luísa Carvalho, Carlos M. G. A. Fontes, and Pedro Bule. "A dual cohesin–dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome." Journal of Biological Chemistry. 296 (2021): 100552. AbstractWebsite

The Cellulosome is an intricate macromolecular protein complex that centralizes the cellulolytic efforts of many anaerobic microorganisms through the promotion of enzyme synergy and protein stability. The assembly of numerous carbohydrate processing enzymes into a macromolecular multiprotein structure results from the interaction of enzyme-borne dockerin modules with repeated cohesin modules present in noncatalytic scaffold proteins, termed scaffoldins. Cohesin–dockerin (Coh-Doc) modules are typically classified into different types, depending on structural conformation and cellulosome role. Thus, type I Coh-Doc complexes are usually responsible for enzyme integration into the cellulosome, while type II Coh-Doc complexes tether the cellulosome to the bacterial wall. In contrast to other known cellulosomes, cohesin types from Bacteroides cellulosolvens, a cellulosome-producing bacterium capable of utilizing cellulose and cellobiose as carbon sources, are reversed for all scaffoldins, i.e., the type II cohesins are located on the enzyme-integrating primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldins. It has been previously shown that type I B. cellulosolvens interactions possess a dual-binding mode that adds flexibility to scaffoldin assembly. Herein, we report the structural mechanism of enzyme recruitment into B. cellulosolvens cellulosome and the identification of the molecular determinants of its type II cohesin–dockerin interactions. The results indicate that, unlike other type II complexes, these possess a dual-binding mode of interaction, akin to type I complexes. Therefore, the plasticity of dual-binding mode interactions seems to play a pivotal role in the assembly of B. cellulosolvens cellulosome, which is consistent with its unmatched complexity and size.

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Esteves, Carina, Susana I. C. J. Palma, Henrique M. A. Costa, Cláudia Alves, Gonçalo M. C. Santos, Efthymia Ramou, Ana Luísa Carvalho, Vitor Alves, and Ana C. A. Roque. "{Tackling Humidity with Designer Ionic Liquid-Based Gas Sensing Soft Materials}." Advanced Materials (2022). Abstract

Relative humidity is simultaneously a sensing target and a contaminant in gas and volatile organic compound (VOC) sensing systems, where strategies to control humidity interference are required. An unmet challenge is the creation of gas-sensitive materials where the response to humidity is controlled by the material itself. Here, humidity effects are controlled through the design of gelatin formulations in ionic liquids without and with liquid crystals as electrical and optical sensors, respectively. In this design, the anions [DCA]− and [Cl]− of room temperature ionic liquids from the 1-butyl-3-methylimidazolium family tailor the response to humidity and, subsequently, sensing of VOCs in dry and humid conditions. Due to the combined effect of the materials formulations and sensing mechanisms, changing the anion from [DCA]− to the much more hygroscopic [Cl]−, leads to stronger electrical responses and much weaker optical responses to humidity. Thus, either humidity sensors or humidity-tolerant VOC sensors that do not require sample preconditioning or signal processing to correct humidity impact are obtained. With the wide spread of 3D- and 4D-printing and intelligent devices, the monitoring and tuning of humidity in sustainable biobased materials offers excellent opportunities in e-nose sensing arrays and wearable devices compatible with operation at room conditions.

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Freire, Filipe, Maria Joao Romao, Anjos L. Macedo, Susana S. Aveiro, Brian J. Goodfellow, and Ana Luisa Carvalho. "Preliminary structural characterization of human SOUL, a haem-binding protein." Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 65 (2009): 723-726. Abstract
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