Due to the rapid progress of biological networks for modeling biological systems, a lot of biomolecular networks have been producing more and more protein-protein interaction (PPI) data. Analyzing protein-protein interaction networks aims to find regions of topological and functional (dis)similarities between molecular networks of different species. The study of PPI networks has the potential to teach us as much about life process and diseases at the molecular level. Although few methods have been developed for multiple PPI network alignment and thus, new network alignment methods are of a compelling need. In this paper, we propose a novel algorithm for a global alignment of multiple protein-protein interaction networks called MAPPIN. The latter relies on information available for the proteins in the networks, such as sequence, function, and network topology. Our algorithm is perfectly designed to exploit current multi-core CPU architectures, and has been extensively tested on a real data (eight species). Our experimental results show that MAPPIN significantly outperforms NetCoffee in terms of coverage. Nevertheless, MAPPIN is handicapped by the time required to load the gene annotation file. An extensive comparison versus the pioneering PPI methods also show that MAPPIN is often efficient in terms of coverage, mean entropy, or mean normalized.