Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. It codes for several cell surface Als (agglutinin-like sequence) glycoproteins (Als1-Als7 and Als9) which are key virulence factor and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. The N-terminal domain of Als proteins (NT-Als) is involved in adhesive function and comprises two tandem DEv-IgG type immunoglobulin domains, N1 and N2, arranged in a fold similar to that of the MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules) domain. It also possesses a peptide-binding cavity (PBC) that can bind peptides with broad specificity.