Issue 8, 2008

Interactions of aluminium hydrolytic species with biomolecules

Abstract

In this contribution the formation of bioinorganic assemblies between the basic globular protein lysozyme and aqueous aluminium species including Al13-mer, Al30-mer and colloidal aluminium hydroxide have been explored and comparison made to previous interaction studies performed with bovine serum albumin (BSA). Specific charge-stabilised bioinorganic assemblies involving aluminium species and lysozyme were observed to form in contrast to the gel like structures formed on interaction of BSA with aluminium species. As demonstrated by infrared spectroscopy (structural assignment, 2D correlation spectroscopy), interactions mostly involve acidic surface groups of the proteins (Asp, Glu), with strong complexation and deprotonation in the case of BSA interacting with Al13 and Al30 and through hydrogen bonding for lysozyme interacting with the same species and aluminium hydroxide particles interacting with both biomolecules.

Graphical abstract: Interactions of aluminium hydrolytic species with biomolecules

Supplementary files

Article information

Article type
Paper
Submitted
31 Mar 2008
Accepted
12 Jun 2008
First published
03 Jul 2008

New J. Chem., 2008,32, 1346-1353

Interactions of aluminium hydrolytic species with biomolecules

O. Deschaume, A. Fournier, K. L. Shafran and C. C. Perry, New J. Chem., 2008, 32, 1346 DOI: 10.1039/B805406C

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements