Interaction of aluminium hydrolytic species with biomolecules

Deschaume, O., Fournier, A.C., Shafran, K.L. and Perry, C.C. ORCID: 0000-0003-1517-468X, 2008. Interaction of aluminium hydrolytic species with biomolecules. New Journal of Chemistry, 32 (8), pp. 1346-1353. ISSN 1144-0546

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Abstract

In this contribution the formation of bioinorganic assemblies between the basic globular protein lysozyme and aqueous aluminium species including Al 13 -mer, Al 30 -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 Al 13 and Al 30 and through hydrogen bonding for lysozyme interacting with the same species and aluminium hydroxide particles interacting with both biomolecules.

Item Type:	Journal article
Publication Title:	New Journal of Chemistry
Creators:	Deschaume, O., Fournier, A.C., Shafran, K.L. and Perry, C.C.
Publisher:	Royal Society of Chemistry
Date:	2008
Volume:	32
Number:	8
ISSN:	1144-0546
Rights:	© Royal Society of Chemistry 2008
Divisions:	Schools > School of Science and Technology
Record created by:	EPrints Services
Date Added:	09 Oct 2015 09:54
Last Modified:	09 Jun 2017 13:13
URI:	https://irep.ntu.ac.uk/id/eprint/4510

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