Solid-state NMR studies of biomineralization peptides and proteins.
Nature has evolved sophisticated strategies for engineering hard tissues through the interaction of proteins, and ultimately cells, with inorganic mineral phases. This process, called biomineralization, is how living organisms transform inorganic materials such as hydroxyapatite, calcite, and silica into highly intricate and organized structures. The remarkable material properties of shell, bone, and teeth come from the activities of proteins that function at the organic-inorganic interface. A better understanding of the biomolecular mechanisms used to promote or retard the formation of mineral-based structures could provide important design principles for the development of calcification inhibitors and promoters in orthopedics, cardiology, urology, and dentistry. With the knowledge of the structural basis for control of hard tissue growth by proteins, scientists could potentially develop materials using biomimetic principles with applications in catalysis, biosensors, electronic devices, and chromatographic separations, to name a few. Additionally, biomineralization also has potential applications in electronics, catalysis, magnetism, sensory devices, and mechanical design. Where man-made hard materials require the use of extreme temperatures, high pressure, and pH, biological organisms can accomplish these feats at ambient temperature and at physiological pH. Despite the fact that many researchers want to identify and control the structure of proteins at material and biomineral interfaces, there is a decided lack of molecular-level structure information available for proteins at biomaterial interfaces in general. In particular, this holds for mammalian proteins that directly control calcification processes in hard tissue. The most fundamental questions regarding the secondary and tertiary structures of proteins adsorbed to material surfaces, how proteins catalyze the formation of biomineral composites, or how proteins interact at biomaterial interfaces remain unanswered. This is largely due to a lack of methods capable of providing high-resolution structural information for proteins adsorbed to material surfaces under physiologically relevant conditions. In this Account, we highlight recent work that is providing insight into the structure and crystal recognition mechanisms of a salivary protein model system, as well as the structure and interactions of a peptide that catalyzes the formation of biosilica composites. To develop a better understanding of the structure and interactions of proteins in biomaterials, we have used solid-state NMR techniques to determine the molecular structure and dynamics of proteins and peptides adsorbed onto inorganic crystal surfaces and embedded within biomineral composites. This work adds to the understanding of the structure and crystal recognition mechanisms of an acidic human salivary phosphoprotein, statherin.
Department of Chemistry, University of Washington , Box 351700, Seattle, Washington 98195, United States.
Adrienne
A
Roehrich
Gary
G
Drobny
D002119:Calcium Carbonate / Q000737:chemistry; D017886:Durapatite / Q000037:antagonists & inhibitors / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012471:Salivary Proteins and Peptides / Q000737:chemistry; D012822:Silicon Dioxide / Q000737:chemistry
D010455:Peptides; D011506:Proteins; C018149:STATH protein, human; D012471:Salivary Proteins and Peptides; D012822:Silicon Dioxide; D017886:Durapatite; D002119:Calcium Carbonate