The objective of our research is to apply lessons learnt from biology in the manipulation of materials chemistry to laboratory studies aimed at generating oxides/ metals with defined size and form. The focus of our work has been on peptide interactions with silica and zinc oxide. Detailed quantitative experimental studies together with molecular modeling studies have shown that G12 (GLHVMHKVAPPR) and GT16 (GLHVMHKVAPPRGGGC) control ZnO morphology by an adsorption mechanism that varies between crystal faces. In contrast, similar peptides, EM 12 (EAHVMHKVAPRP) and EC12 (EAHVCHKVAPRP) were found to control ZnO formation via the retention of Zn(II) in solution. Differences between the behaviour of the two peptides arose from the availability of the sulphur atom for complex formation. A series of peptides identified by the phage display against specific sizes of amorphous silica particles showed relationships between fundamental properties of the peptides themselves (e.g. pi and hydrophobicity) and surface binding. The effect of single point mutations (Ala for His) in an individual silica binding peptide (KSLSRHDHIHHH) were explored by experiment and modeling (MD and QM studies) and showed the importance of peptide flexibility for effective surface binding.