Journal of Spectroscopy

Journal of Spectroscopy / 2010 / Article
Special Issue

From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 1 of 2

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Open Access

Volume 24 |Article ID 263012 | 5 pages | https://doi.org/10.3233/SPE-2010-0424

The role of Lys525 on the head-group anchoring of fatty acids in the highest affinity binding site of albumin

Abstract

Human serum albumin provides the transport of long-chain fatty acids in the blood through three high-affinity and four low-affinity binding sites. Molecular dynamics simulations have been performed to investigate the anchoring of palmitic acid molecules to the protein. In the site with the highest affinity, Site 5, the key residue Lys525 not only binds the head-group of the palmitate ion by electrostatic interactions with its charged terminal group, but it also accommodates the first portion of the lipid chain by non-electrostatic interactions with the rest of its sidechain. The flexibility of Lys525, and in particular of the dihedral angle χ3, is suggested to account for a number of spectroscopic properties observed in correspondence with the entrance of the hydrophobic pocket constituting Site 5.

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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