Identification of inorganic crystal-specific sequences using phage display combinatorial library of short peptides: A feasibility study

The feasibility of using a combinatorial phage display library of decapeptides to identify ligands which can interact with the surface of a crystal was assessed using geological calcium carbonate as a model. Two relatively strong binding clones were identified by ELISA, sequenced and the encoded oligopeptides were prepared by solid phase synthesis and their properties compared with those of casein hydrolysate.

[1]  C. Alexander,et al.  Directed nucleation of calcite at a crystal-imprinted polymer surface , 1999, Nature.

[2]  Y. Yeh,et al.  Antifreeze proteins: Current status and possible food uses , 1998 .

[3]  S. Weiner,et al.  Interactions of sea-urchin skeleton macromolecules with growing calcite crystals— a study of intracrystalline proteins , 1988, Nature.

[4]  S. Weiner,et al.  Intercalation of sea urchin proteins in calcite: study of a crystalline composite material. , 1990, Science.

[5]  S. Weiner,et al.  Control and Design Principles in Biological Mineralization , 1992 .

[6]  V. Gerbaud,et al.  Mechanism of Calcite Crystal Growth Inhibition by the N-terminal Undecapeptide of Lithostathine* , 2000, The Journal of Biological Chemistry.

[7]  S. Weiner,et al.  Control of Aragonite or Calcite Polymorphism by Mollusk Shell Macromolecules , 1996, Science.

[8]  P. C. Rieke,et al.  Innovative materials processing strategies: a biomimetic approach. , 1992, Science.

[9]  X. H. Wu,et al.  Control of crystal phase switching and orientation by soluble mollusc-shell proteins , 1996, Nature.

[10]  K. Larsson.  Tailoring lipid functionality in foods , 1994 .

[11]  Stephen Mann,et al.  Molecular tectonics in biomineralization and biomimetic materials chemistry , 1993, Nature.

[12]  P. Lillford,et al.  A carrot leucine-rich-repeat protein that inhibits ice recrystallization. , 1998, Science.

[13]  S. Weiner,et al.  Acidic macromolecules of mineralized tissues: the controllers of crystal formation. , 1991, Trends in biochemical sciences.

[14]  Y. Liou,et al.  Hyperactive antifreeze protein from beetles , 1997, Nature.

[15]  Stephen Mann,et al.  Morphological influence of functionalized and non-functionalized α,ω-dicarboxylates on calcite crystallization , 1990 .

[16]  T. Koetzle,et al.  Biological Control of Crystal Texture: A Widespread Strategy for Adapting Crystal Properties to Function , 1993, Science.

[17]  P. Dove,et al.  Thermodynamics of calcite growth: baseline for understanding biomineral formation , 1998, Science.

[18]  R. Hartel.  Ice crystallization during the manufacture of ice cream , 1996 .

[19]  Z. Jia,et al.  Structural basis for the binding of a globular antifreeze protein to ice , 1996, Nature.

[20]  L. Addadi,et al.  Antibodies against crystals , 1992, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[21]  F. Sicheri,et al.  Ice-binding structure and mechanism of an antifreeze protein from winter flounder , 1995, Nature.

[22]  S. Mann,et al.  Crystallization at Inorganic-organic Interfaces: Biominerals and Biomimetic Synthesis , 1993, Science.

[23]  George M. Whitesides,et al.  Control of crystal nucleation by patterned self-assembled monolayers , 1999, Nature.

[24]  R. Laursen,et al.  CONTROL OF CALCITE CRYSTAL MORPHOLOGY BY A PEPTIDE DESIGNED TO BIND TO A SPECIFIC SURFACE , 1997 .