Five oligopeptides-glycylglycine, glycyl-l-asparagine, glutathione, glycyl-l-prolyl-l-alanine, and glycyl-l-prolyl-glycyl-glycine-were crystallized epitaxially from solution on a variety of alkali halide (001) cleavage faces. Morphological observations, in conjunction with knowledge of the crystal structure of the first three compounds, have enabled some inferences to be drawn on molecular orientations upon the substrate surface. Comparisons have been made between the epitaxial crystallization of these oligopeptides and the oriented overgrowths formed by chain macromolecules on the same surfaces. From these studies it can be shown that some di-, tri-, and tetrapeptides, which are representative of important amino acid sequences in collagen, exhibit a specific and positive mode of association on a mineral surface.
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Colloid and Surface Chemistry