Efficient Gene Transfection through Inhibition of β‐Sheet (Amyloid Fiber) Formation of a Short Amphiphilic Peptide by Gold Nanoparticles. Issue 28 (10th April 2017)

• Record Type: Journal Article
• Authors: Jana, Poulami; Samanta, Krishnananda; Bäcker, Sandra; Zellermann, Elio; Knauer, Shirley; Schmuck, Carsten
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 28(2017)
• Page Start: 8083
• Page End: 8088
• Publication Date: 2017-04-10
• Subjects: amyloid fibers -- beta sheet formation -- gene delivery -- nanoparticles -- self-assembly; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201700713
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The effect of citrate‐stabilized gold nanoparticles (AuNPs) on the secondary structure of an artificial β‐sheet‐forming cationic peptide has been studied. The AuNPs inhibited β‐sheet formation and led to fragmented fibrils and spherical oligomers with assembled AuNPs on their surface. Besides this structural change, the functional properties of the peptide are also different. Whereas the peptide was unable to act as a vector for gene delivery, formation of a complex with AuNPs allowed successful gene delivery into cells. Abstract : Call the tune : Negatively charged gold nanoparticles (AuNPs) have been found to inhibit the ability of cationic amphiphilic peptide1 to form β‐sheet structures and also induce disruption of the aggregates. Furthermore, they also tune the functional properties of the peptide, with the complex being an efficient gene transfection vector whereas the peptide by itself is not.