Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.

The flexibility of the ATP synthase's β subunit promotes its role in the ATP synthase rotational mechanism, but its domains stability remains unknown. A reversible thermal unfolding of the isolated β subunit (Tβ) of the ATP synthase from Bacillus thermophilus PS3, tracked through circular dichroism and molecular dynamics, indicated that Tβ shape transits from an ellipsoid to a molten globule through an ordered unfolding of its domains, preserving the β-sheet residual structure at high temperature. We determined that part of the stability origin of Tβ is due to a transversal hydrophobic array that crosses the β-barrel formed at the N-terminal domain and the Rossman fold of the nucleotide-binding domain (NBD), while the helix bundle of the C-terminal domain is the less stable due to the lack of hydrophobic residues, and thus the more flexible to trigger the rotational mechanism of the ATP synthase.

Improving coarse-grained models of protein folding through weighting of polar-polar/hydrophobic-hydrophobic interactions into crowded spaces.

Herein were tested 7 hydrophobic-polar sequences in two types of 2D-square space lattices, homogeneous and correlated, the latter simulating molecular crowding included as a geometric boundary restriction. Optimization of 2D structures was carried out using a variant of Dill's model, inspired by convex function, taking into account both hydrophobic (Dill's model) and polar interactions, including more structural information to reach better folding solutions. While using correlated networks, degrees of freedom in the folding of sequences were limited; as a result in all cases, more successful structural trials were found in comparison to a homogeneous lattice.

Nanostructured oleic acid/polysorbate 80 emulsions with diminished toxicity in NL-20 cell line: Insights of potential drug carriers.

Nanoemulsions (NE) are nowadays required drug nanocarriers. We have selected i) oleic acid (OA) as oil (O), ii) polysorbate 80 (PS) as surfactant (S), and iii) water (W) in a prototype NE. Our best formulation had O:S ratio [OA]/[PS] = 0.

In silico minimalist approach to study 2D HP protein folding into an inhomogeneous space mimicking osmolyte effect: First trial in the search of foldameric backbones.

We have employed our bioinformatics workbench, named Evolution, a Multi-Agent System based architecture with lattice-bead-models, evolutionary-algorithms, and correlated-networks as inhomogeneous spaces, with different correlation lengths, mimicking osmolyte effect (molecular crowding), to in silico survey protein folding. Resolution is with hydrophobic-polar (H-P) sequences in inhomogeneous 2D square lattices, since general biophysicochemical trends consider i) that the backbone is one of the major components responsible for protein folding and ii) osmolyte effect plays an important role to better folding kinetics and reach deeper optima. We have designed foldamers, as square n × n (n = 3, 4, 5, 6) arrays of hydrophobic cores stabilized by H⋯H contacts, attached through short PP (P) or long PPPP (P) loops, giving rise to 8 sequences (S to S) with known optimal scores.