Study on physisorption between G‐actin and amphiphilic polymer‐coated gold nanoparticles

Abstract

Physisorptions occurs everywhere and constantly in living organisms and between nanomaterials and biomolecules. In this study, one of the most important proteins, G-actin, was selected to investigate its bio-nano physisorption with a model nanoparticle coated with a amphiphilic polymer. Using a photoluminescence quenching method, both the binding constant and the Hill constant were determined as 1.79 × 10 M and 0.84, respectively. Thermodynamic calculations proved that such a physisorption was a spontaneous procedure. The physisorption-mediated protein-nanoparticle conjugates were robust enough to resist gel electrophoresis, and protein conformation was kept intact, as revealed using circular dichroism. This conjugate might be a promising candidate for nanofabrication or could play a significant role in actin-related bioactivities.

A study on human serum albumin corona formed on photoluminescent carbon dots

“…This method refers to previous publications with minor modifications. 27–29,34–35 In brief, the excitation was fixed at 280 nm and the slits for both excitation and emission were set at 5.0 nm in all PL measurements. The temperature was controlled by a water bath and the samples were incubated for at least 30 min.…”

“…25 By choosing PCDs and HSA as two model materials, in this paper, we have investigated the interactions between HSA and our "home-made" PCDs prepared from citric acids. By employing both the fluorescence quenching method based on the fluorescence resonance energy transfer (FRET) [27][28][29][30][31][32] and spectrum superimposition, the binding constants and the number of binding sites have been determined. In addition, the corresponding thermodynamics for the PCD-HSA interaction are discussed.…”

Creating de novo peptide-based bioactivities: from assembly to origami

“…In cells, peptides form versatile nanostructures with different bioactivities through self-assembly and co-assembly. Proteins such as collagen, 1 actin 2 and the peptides/proteins that are associated with amyloid diseases 3 can self-assemble into fibrous structures. Helicase 4 and nuclease 5 are naturally ring-shaped structures.…”