3752878

Crowding agents stabilize supramolecular assembly

Date
August 23, 2022

Supramolecules such as, octa-acid (OA), tetra-endo-methyl octa-acid (TEMOA) and Positand are host molecules that possesses a water-soluble outer coat and a deep hydrophobic pocket suitable for binding a range of non-polar guests in aqueous solution. Via the hydrophobic effect, OA readily assembles into dimeric capsules in the presence of suitably sized guests. However, experiments have shown that the Positand does not assemble into complexes as easily as OA. In studies involving macromolecular crowding, effects that have been observed include formation of macromolecular complexes in solution and the stabilization of folded proteins and protein/ligand complexes. The magnitude of the effect has been shown to strongly depend upon the relative sizes and shapes of concentrated crowding species. Here, we study via molecular simulation techniques, the impact of molecular crowders on the assembly properties of supramolecules. Our approach was to create different simulation systems at different temperatures all below the LCST of the crowders. Our results so far show that the type, concentration and/ or molecular weight of the crowding agent molecule in the simulation system, relatively impacts the supramolecular complex stabilization.

Speakers

Speaker Image for Bruce Gibb
Professor, Tulane University

Related Products

Thumbnail for Use local reporting to characterize the thermodynamics signatures of β-turns and carboxylic acids/ carboxylates | Poster Board #829
Use local reporting to characterize the thermodynamics signatures of β-turns and carboxylic acids/ carboxylates | Poster Board #829
Heat denaturation of proteins is intuitive. Any process induced by increasing temperature should proceed with an increased enthalpy and entropy of the system. However, ordered globular proteins can also be disrupted by cooling, and exhibit a temperature of maximum stability…
Thumbnail for Anion binding induced denaturation of β-hairpins: Implications for the salting-in Hofmeister Effect | Poster Board #813
Anion binding induced denaturation of β-hairpins: Implications for the salting-in Hofmeister Effect | Poster Board #813
Although appreciated for almost 140 years, the detailed mechanism by which anions can induce the salting-in of proteins and peptides remains unclear…
Thumbnail for Anion affinity and aggregation of N-terminal a-synuclein15 peptides | Poster Board #207
Anion affinity and aggregation of N-terminal a-synuclein15 peptides | Poster Board #207
a-Synuclein (α-Syn) is an intrinsically disordered protein linked to the pathogenesis of Parkinson's disease (PD) by its misfolding, aggregation, and accumulation in Lewy bodies; the characteristic amyloids of PD…