Conformational studies of peptide-amphiphiles based on hydroxyapatite nucleation motifs

Nathan Lockwood; Kevin H Mayo; Matthew Tirrell

Conformational studies of peptide-amphiphiles based on hydroxyapatite nucleation motifs

Nathan Lockwood, Kevin H Mayo, Matthew Tirrell

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article

Abstract

Our work centers on understanding the stereochemical relationships between these domains and hydroxyapatite crystals in order to extrapolate the underlying principles to new biomaterials. We have incorporated several short phosphoryn protein sequences and analog into 'peptide-amphiphiles' by covalently linking the N-terminus of the peptide to lipid tails. The combination of CD and NMR structural data and nucleation properties will eventually be used to develop a model of the stereochemical relationships between peptide templates and hydroxyapatite crystals.

Original language	English (US)
Journal	Annals of Biomedical Engineering
Volume	28
Issue number	SUPPL. 1
State	Published - Dec 1 2000

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title = "Conformational studies of peptide-amphiphiles based on hydroxyapatite nucleation motifs",

abstract = "Our work centers on understanding the stereochemical relationships between these domains and hydroxyapatite crystals in order to extrapolate the underlying principles to new biomaterials. We have incorporated several short phosphoryn protein sequences and analog into 'peptide-amphiphiles' by covalently linking the N-terminus of the peptide to lipid tails. The combination of CD and NMR structural data and nucleation properties will eventually be used to develop a model of the stereochemical relationships between peptide templates and hydroxyapatite crystals.",

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N2 - Our work centers on understanding the stereochemical relationships between these domains and hydroxyapatite crystals in order to extrapolate the underlying principles to new biomaterials. We have incorporated several short phosphoryn protein sequences and analog into 'peptide-amphiphiles' by covalently linking the N-terminus of the peptide to lipid tails. The combination of CD and NMR structural data and nucleation properties will eventually be used to develop a model of the stereochemical relationships between peptide templates and hydroxyapatite crystals.

AB - Our work centers on understanding the stereochemical relationships between these domains and hydroxyapatite crystals in order to extrapolate the underlying principles to new biomaterials. We have incorporated several short phosphoryn protein sequences and analog into 'peptide-amphiphiles' by covalently linking the N-terminus of the peptide to lipid tails. The combination of CD and NMR structural data and nucleation properties will eventually be used to develop a model of the stereochemical relationships between peptide templates and hydroxyapatite crystals.

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