Nature-based and sustainably sourced cosmetics have been dominating the area of skincare products worldwide. Due to their antioxidant and antiaging properties, compounds from cyanobacteria, such as carotenoids and phycobiliproteins, may replace synthetic ingredients in cosmetic formulations and may be used in products such as sunscreens, skincare creams, and makeup. In this study, we evaluated the potential of acetonic and aqueous extracts from cyanobacteria strains of the genera Cyanobium and Leptothoe and from strains within Synechococcales and Oscillatoriales orders, for use in cosmetics. Extractions were sequentially performed with acetone and water. Extracts were firstly analyzed for their toxicity to keratinocytes, fibroblasts, and endothelial cells (HaCAT, 3T3L1 and hCMEC/D3, respectively). The non-cytotoxic extracts were characterized in terms of total proteins, carotenoids, chlorophyll, phenols, phycobiliproteins, and analyzed for their antioxidant potential against the superoxide anion radical (O₂^•−), and for their ability to inhibit key enzymes associated with the skin aging process. Aqueous extracts were richer in total proteins and phycobiliproteins. The aqueous extracts of Synechococcales cyanobacterium LEGE 181157 and Synechococcales cyanobacterium LEGE 181150 showed the highest value for total proteins (760.81 and 695.25 μg BSA mL⁻¹_{dry extract,} respectively) and the best values regarding O₂^•− scavenging (IC₅₀ = 63.24 and 112.18 μg mL⁻¹_{dry extract}, respectively) with a significant negative correlation observed (p < 0.01). Moreover, aqueous extracts of Synechococcales cyanobacterium LEGE 181150 and Synechococcales cyanobacterium LEGE 181157 inhibited hyaluronidase, (IC₅₀ of 483.86 and 645.06 μg mL⁻¹_{dry extract}, respectively), with a significant negative correlation with total proteins (p < 0.05), pointing out the contribution of these compounds to the biological activities observed. Acetonic extracts were richer in carotenoids and phenols. Zeaxanthin and β-carotene were predominant among all strains, being present in higher amount in Cyanobium sp. LEGE 07175 (53.08 μg mg⁻¹) and Leptothoe sp. LEGE 181156 (47.89 μg mg⁻¹), respectively. The same strains also showed the highest values for collagenase inhibition at 750 μg mL⁻¹_{dry extract} (32.88 and 36.61%, respectively). Furthermore, Leptothoe sp. LEGE 181156 exhibited the lowest IC₅₀ value for tyrosinase inhibition (465.92 μg mL⁻¹_{dry extract}) and Synechococcales cyanobacterium LEGE 181157 presented the best values for elastase inhibition (IC₅₀ of 380.50 and IC₂₅ of 51.43 μg mL⁻¹_{dry extract}). In general, cyanobacteria extracts demonstrated potential for being used for antiaging purposes, with aqueous extracts being more efficient at free radicals scavenging and acetonic ones at avoiding degradation of dermal matrix components.

Conus ateralbus is a cone snail endemic to the west side of the island of Sal, in the Cabo Verde Archipelago off West Africa. We describe the isolation and characterization of the first bioactive peptide from the venom of this species. This 30AA venom peptide is named conotoxin AtVIA (δ-conotoxin-like). An excitatory activity was manifested by the peptide on a majority of mouse lumbar dorsal root ganglion neurons. An analog of AtVIA with conservative changes on three amino acid residues at the C-terminal region was synthesized and this analog produced an identical effect on the mouse neurons. AtVIA has homology with δ-conotoxins from other worm-hunters, which include conserved sequence elements that are shared with δ-conotoxins from fish-hunting Conus. In contrast, there is no comparable sequence similarity with δ-conotoxins from the venoms of molluscivorous Conus species. A rationale for the potential presence of δ-conotoxins, that are potent in vertebrate systems in two different lineages of worm-hunting cone snails, is discussed.

Marine Cone snails of the genus Conus contain complex peptide toxins in their venom. Living in tropical habitats, they usually use the powerful venom for self-defense and prey capture. Here, we study Conus crotchii venom duct using a peptide mass-matching approach. The C. crotchii was collected on the Cape Verde archipelago in the Boa Vista Island. The venom was analyzed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). About 488 molecular masses between 700 Da and 3000 Da were searched bymatching with known peptide sequences from UniProtKB protein sequence database. Through this method we were able to identify 12 conopeptides. For validation we considered the error between the experimental molecular mass (monoisotopic) and the calculated mass of less than 0.5 Da. All conopeptides detected belong to the A-, O1-, O2-, O3-, T- and D-superfamilies, which can block Ca²⁺ channels, inhibit K⁺ channels and act on nicotinic acetylcholine receptors (nAChRs). Only a few of the detected peptides have a 100% UniProtKB database similarity, suggesting that several of them could be newly discovered marine drugs.

The aim of this study was to document the biodiversity of cyanobacteria genera isolated from intertidal and subtidal zones in Cabo Verde. The identification of the strains was conducted using a polyphasic study, comprising 16S rRNA gene maximum likelihood and Bayesian inference phylogeny, 16S rRNA identity (p-distance), 16S–23S ITS secondary structure, morphological, and habitat analyses. A total of 51 strains were isolated by micromanipulation and by streaking biomass onto Petri dishes with a solid medium. Seventeen strains were identified as belonging to the Salileptolyngbya genus and five to Leptothoe; sixteen strains were distributed across twelve genera. Thirteen strains were grouped into eight distinct clades, but could not be assigned to any cyanobacterial genus, indicating that they could be described as new cyanobacterial genera in the future. The phylogenies also exhibited isolates LEGE 181157, LEGE 181224, and LEGE 181227 clustered with Gibliniella, but in a separate clade from the G. alaskensis type. The 16S rRNA gene identity values among these new isolates and G. alaskensis ranged from 94.4% to 95.5%. The 16S–23S ITS dissimilarity between LEGE 181224 and G. alaskensis was 9.4%. Morphologically, these three LEGE strains differ from G. alaskensis in that they have trichomes that are never coiled and have diffluent mucilaginous envelopes, whereas G. alaskensis has coiled trichomes with firm sheaths. Based on these strains, we describe here a new species of Gibliniella.

The venom of cone snails has been proven to be a rich source of bioactive peptides that target a variety of ion channels and receptors. α-Conotoxins (αCtx) interact with nicotinic acetylcholine receptors (nAChRs) and are powerful tools for investigating the structure and function of the various nAChR subtypes. By studying how conotoxins interact with nAChRs, we can improve our understanding of these receptors, leading to new insights into neurological diseases associated with nAChRs. Here, we describe the discovery and characterization of a novel conotoxin from Conus ateralbus, αCtx-AtIA, which has an amino acid sequence homologous to the well-described αCtx-PeIA, but with a different selectivity profile towards nAChRs. We tested the synthetic αCtx-AtIA using the calcium imaging-based Constellation Pharmacology assay on mouse DRG neurons and found that αCtx-AtIA significantly inhibited ACh-induced calcium influx in the presence of an α7 positive allosteric modulator, PNU-120596 (PNU). However, αCtx-AtIA did not display any activity in the absence of PNU. These findings were further validated using two-electrode voltage clamp electrophysiology performed on oocytes overexpressing mouse α3β4, α6/α3β4 and α7 nAChRs subtypes. We observed that αCtx-AtIA displayed no or low potency in blocking α3β4 and α6/α3β4 receptors, respectively, but improved potency and selectivity to block α7 nAChRs when compared with αCtx-PeIA. Through the synthesis of two additional analogs of αCtx-AtIA and subsequent characterization using Constellation Pharmacology, we were able to identify residue Trp18 as a major contributor to the activity of the peptide.