The amphiphilic hydrophobin Vmh2 plays a key role in one step synthesis of hybrid protein-gold nanoparticles.

Colloids Surf B Biointerfaces

Sorbonne Universités, UPMC Paris 06, Laboratoire de Réactivité de Surface, 4 place Jussieu, Paris F-75005, France; CNRS, UMR 7197, Laboratoire de Réactivité de Surface, Paris F-75005, France.

Published: December 2015


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

We report a simple and original method to synthesize gold nanoparticles in which a fungal protein, the hydrophobin Vmh2 from Pleurotus ostreatus and dicarboxylic acid-terminated polyethylene-glycol (PEG) has been used as additional components in a one step process, leading to hybrid protein-metal nanoparticles (NPs). The nanoparticles have been characterized by ultra-violet/visible, infrared and X-ray photoelectron spectroscopies, dynamic light scattering and also by electron microscopy imaging. The results of these analytical techniques highlight nanometric sized, stable, hybrid complexes of about 12 nm, with outer surface rich in functional chemical groups. Interaction with protein and antibodies has also been exploited.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.colsurfb.2015.09.021DOI Listing

Publication Analysis

Top Keywords

hydrophobin vmh2
8
amphiphilic hydrophobin
4
vmh2 plays
4
plays key
4
key role
4
role step
4
step synthesis
4
synthesis hybrid
4
hybrid protein-gold
4
nanoparticles
4

Similar Publications

Article Synopsis
  • - Hydrophobins are specialized proteins that help fungal mycelium manage its interaction with air and surrounding mediums, with specific genes identified in the fungus Pleurotus ostreatus, particularly those encoding Vmh2, Vmh3, and Hydph16, which play key roles in its growth.
  • - The study found that deleting the gene for Hydph16 resulted in a significant reduction in aerial mycelium density and a 40% decrease in cell wall thickness compared to control strains, while leaving major cell wall polysaccharide components intact.
  • - Unlike Vmh2 and Vmh3, the absence of Hydph16 did not affect mycelial hydrophobicity, indicating that different hydrophobins
View Article and Find Full Text PDF

The main aim of this work is to account for the prevention and control of microbial growth on surfaces of interest in medical technology. Surface modification is often achieved by physiotherapy or chemical treatments that can involve time-consuming steps, hazardous reagents, and harsh conditions. One of the ways to overcome these drawbacks is the use of surface-active proteins such as hydrophobins.

View Article and Find Full Text PDF

Fungi produce surface-active proteins, among which hydrophobins are the most characterized and attractive also for their ability to form functional amyloids. Our most recent findings show that these abilities are shared with other classes of fungal proteins. Indeed, in this paper, we compared the characteristics of a class I hydrophobin (Vmh2 from ) and an unknown protein (named PAC3), extracted from the marine fungal strain which does not belong to the same protein family based on its sequence features.

View Article and Find Full Text PDF

Hydrophobins, which are small-secreted proteins with both hydrophobic and hydrophilic parts, can self-assemble into an amphiphilic film at the air-water interface, helping the fungus to form aerial hyphae. In the agaricomycete Pleurotus ostreatus, more than 20 putative hydrophobin genes have been predicted. Of these, two hydrophobin genes, vmh2 and vmh3, are predominantly expressed in the vegetative mycelium.

View Article and Find Full Text PDF