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In an ever-changing world, learning becomes a necessity, not an option. But how to ensure that we are prepared for the new realities? Is what we learn at school and at work enough? Lifelong Learning emerges as a response to these challenges. Through the autonomous search for knowledge, we go beyond the classroom and discover new possibilities. This article analyzes how explanatory research and bibliographic analysis can help understand lifelong learning, identifying obstacles and promoting personal discoveries. But because some people stop learning? The Lifelong Learning study seeks to understand this issue and encourage the resumption of learning. Curiosity, motivation and adaptability are essential to apply knowledge in practice and stand out in a constantly changing market. Investing time and effort in learning is essential for personal and professional development. It is the key to a promising future in a constantly evolving world. With this, we will increasingly develop the ability to anticipate and predict a new wave. Adopting this practice is challenging, but it will be very rewarding. [ABSTRACT FROM AUTHOR]

Abstract: Sea anemones produce a wide variety of biologically active compounds, such as the proteinaceous neurotoxins and cytolysins. Herein we report a new peptide, purified to homogeneity from the neurotoxic fraction of B. caissarum venom, by using gel filtration followed by rp-HPLC, naming it as BcIV. BcIV is a 41 amino acid peptide (molecular mass of 4669 amu) possessing 6 cysteines covalently linked by three disulfide bonds. This toxin has 45 and 48% of identity when compared to APETx1 and APETx2 from Anthopleura elegantissima, respectively, and 42% of identity with Am-II and BDS-I and-II obtained from Antheopsis maculata and Anemonia sulcata, respectively. This neurotoxin presents only a weak-paralyzing action (minimal Lethal Dose close to 2000 μg/kg) in swimming crabs Callinectes danae. This appears to be a different effect to that caused by the type 1 sea anemone toxin BcIII that is lethal to the same animals at lower doses (LD50 =219 μg/kg). Circular dichroism spectra of BcIII and BcIV show a high content of β-strand secondary structure in both peptides, very similar to type 1 sodium channel toxins from various sea anemones, and to APETx1 and APETx2 from A. elegantissima, a HERG channel modulator and an ASIC3 inhibitor, respectively. Interestingly, BcIII and BcIV have similar effects on the action potential of the crab leg nerves, suggesting the same target in this tissue. As BcIII was previously reported as a Na+ channel effector and BcIV is inactive over Na+ currents of mammalian GH3 cells, we propose a species-specific action for this new molecule. A molecular model of BcIV was constructed using the structure of the APETx1 as template and putative key residues are discussed. [Copyright &y& Elsevier]