title: Phage display for the discovery of hydroxyapatite-associated peptides.
abstract: In nature, proteins play a critical role in the biomineralization process. Understanding how different peptide or protein sequences selectively interact with the target crystal is of great importance. Identifying such protein structures is one of the critical steps in verifying the molecular mechanisms of biomineralization. One of the promising ways to obtain such information for a particular crystal surface is to screen combinatorial peptide libraries in a high-throughput manner. Among the many combinatorial library screening procedures, phage display is a powerful method to isolate such proteins and peptides. In this chapter, we will describe our established methods to perform phage display with inorganic crystal surfaces. Specifically, we will use hydroxyapatite as a model system for discovery of apatite-associated proteins in bone or tooth biomineralization studies. This model approach can be generalized to other desired crystal surfaces using the same experimental design principles with a little modification of the procedures.
authors.affiliation: Department of Bioengineering, University of California, Berkeley, California, USA; Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
authors.forename: Hyo-Eon
authors.initials: HE
authors.lastname: Jin
authors.forename: Woo-Jae
authors.initials: WJ
authors.lastname: Chung
authors.forename: Seung-Wuk
authors.initials: SW
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D017104:Bacteriophage M13 / Q000235:genetics; D002113:Calcification, Physiologic; D017886:Durapatite / Q000737:chemistry*; D004926:Escherichia coli; D005818:Genetic Engineering; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry*; D060327:Solid-Phase Synthesis Techniques
chemical_list: D019151:Peptide Library; D010455:Peptides; D017886:Durapatite
keywords: Biomineralization; Hydroxyapatite; Phage display; Phage engineering; Recognition peptides