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We investigated the adsorption characteristics of an α-helical segment with 12 residues derived from the full protein structure of bovine serum albumin. It was found that the peptide adsorbs onto graphene, leading to significant changes in the helical content. Adsorption onto graphene induces a transition in the peptide, destabilizing the close-packed α-helices to form significant amounts of loose-packed 3₁₀-helices. This is confirmed through comparison of the hydrogen bond formation in the peptide with and without the presence of graphene.

Molecular Dynamics; Bovine Serum Albumin; Graphene; Adsorption; Protein Conformation;