BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
Lecture 12: Organic templating of inorganic materials and bone biomimesis
Last time: interfacial biomineralization and biomimetic inorganic chemistry
Today: biological strategies for inorganic templating by organic materials
Biomimetic organic template materials
Biomimesis of bone
Reading: S. Mann, ‘Biomineralization: Principles and Concepts of Bioinorganic Materials
Chemistry,’ Ch. 6, pp. 89-124 (2001)
Biological strategies for inorganic templating by organic materials
Alteration of barriers to nucleation
? Organic surfaces alter free energy barrier to nucleation (Mann Science 1993)
?G*
?G
nuc
o Reminder of free energy of nucleation (homogeneous, but principle applies to heterogeneous surface
nucleation as well):
?G
nuc
=?G
surface
??G
bulk
= 4πr
2
σ?
4
3
πr
3
?G
v
V
m
null Where ?Gv is the free energy change for formation of the solid per mole from the ions, and Vm is the
molar volume of the nucleated solid
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
? How are free energy barriers modified by organic templates? (Mann 1993) Complementarity in:
1. Surface lattice geometries
2. Spatial charge distributions
3. Polarity of hydration layers
4. Defect sites
5. Bonding chemistry
null Coordination environment of metal ion in crystal mimicked by binding to organic surface groups
o Matching lattice geometries:
Organic templating layer
New crystal
(Mann et al. 1993)
o Matching charge distributions:
null Case of calcium cabonate: different crystal structures and crystal orientations nucleated on different
charge surfaces
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
o Templates used by nature:
null Proteins
null Lipids
null polysaccharides
o Process is universal for templated nucleation:
null Material: carbonates, phosphates silica, ice
null Template: carboxy-rich moieties hydrogen-bonding moieties
o E.g. Aspartic acid, glutamic acid, phorphorylated residues for carboxy-rich
o E.g. polysaccharides, Ser, Thr for hydrogen-bonding residues
null (refs in Mann 1993)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
control of nucleation and growth
? organic templates can preferentially nucleate the inorganic without ordering or aligning it
o e.g. silica deposition in radiolarians and diatoms
? Templated crystal growth needs both recognition of individual molecules and a larger underlying lattice to drive
directed nucleation
o Obtaining periodicity in organic template:
null How nature does it: secondary structures (nm-scale organization): α helix, β sheet
null On larger length scales, cells control deposition
? Localization and orientation of proteins and phospholipids
null Secondary, tertiary, and quarternary protein structures are involved to provide the ‘lattice’ for
templating crystals
? Ordered template geometries may allow selection of crystal polymorph
o Requires flat, ordered surface in 2D
o E.g. for CaCO
3
: calcite vs. aragonite vs. vaterite
Calcium carbone (CaCO
3
) crystal structures
calcite
aragonite
(http://ruby.coloarado.edu/~smyth/min/minerals.html)
null Example: nacre
o Layered CaCO
3
structure of seashells (mollusks, etc.)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
Plate-like aragonite (CaCO
3
) crystals
form the inner layer of seashells:
(scale bar 1 μm)
Biomimetic organic templated materials
Patterned surface mimics of templated inorganics
1
Directed mineral deposition by patterned surfaces presenting organized charged groups
2,3
null Work of Joanna Aizenberg at Bell Labs:
(Aizenberg et al. 2000)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
null Supersaturation theory/model
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
Mimicking the silica deposition of diatoms
nanovesicles
SDV - silica deposition vesicles
AV - aleolar vesicles
PL - plasmalemma (lipid bilayer cell wall)
ER - endoplasmic reticulum
Disk-shaped diatom
Silaffin cationic polypeptide lines
SDVs and provides a nucleating
surface for silica deposition in the
diatom:
SSKKSGSYSGSGSKGSKRR
Amine side chains
(Brott et al. 2001)
Si substrate
(tri-acrylate)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
+ Si(OH)
4
(aq) [10 min. room temp]
Silaffin peptide in grooves of gel surface
Reverse recognition: Using synthetic inorganic materials to guide localization of biological targets
4
(Belcher lab)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
Biomimesis of bone
Structure of human bone
2 component model of organic matrix
null the organic matrix within bone is composed of 2 classes of organic materials
o crystals grown out from nucleating surface composed of acidic macromolecules
component Composition Water
solubility
Role
Framework
macromolecules
Hydrophobic/cross-linked
proteins and polysaccharaides
Low Matrix structural integrity
Acidic
macromolecules
Glycoproteins and
proteoglycans
High Nucleating surface for
hydroxyapatite
null components in human bones:
System Framework macromolecules Acidic macromolecules
Bone and dentine Cross-linked type I collagen Glycoproteins:
fibrils Ostoepontin (these rich in
Osteonectin Asp and Glu)
Proteoglycans:
Chondroitan sulfate
Keratin sulfate
Tooth enamel Amelogenin Glycoproteins:
enamelin
Organization of organic matrix
null framework macromolecules
o tropocollagen cross-linked at helix ends in staggered arrangement
null maximizes interfilament cross-links
o each tropocollagen helix is 280 nm long
o gaps between helices 40 nm x 5 nm ‘hole zones’
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
Human bone framework macromolecules:
Staggered arrangement of tropocollagen (triple helices) maximizes interfilament
cross-links:
null glycoproteins bind collagen
o exact role/organization is not yet known
null structural hierarchy
o TEM micrograph in lamellar bone paper showing plywood structure
5
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
?plywood?arrangement of mineralized
collagen sheets
osteon
Haversian bone -
groups of osteons
null matrix assembly:
(Mann, 2001)
synthetic attempts to mimic bone structure for biomaterials
null Stupp group at Northwestern University
6,7
o Mimicking hydroxyapatite localized growth using a self-assembling peptide amphiphile
o SA peptide forms nanofibers – mimetic in mesoscale structure to collagen fibrils (though formed in a
completely different way)
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BEH.462/3.962J Molecular Principles of Biomaterials Spring 2003
(Hartgerink et al. 2001)
TEM of
Frozen fibers:
TEM of fibers incubated 30 min. in CaCl
2
/Na
2
HPO
4
:
HA aligns with fibril axis
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References
1. Brott, L. L. et al. Ultrafast holographic nanopatterning of biocatalytically formed silica. Nature 413, 291-3 (2001).
2. Aizenberg, J., Black, A. J. & Whitesides, G. M. Control of crystal nucleation by patterned self-assembled
monolayers. Nature 398, 495-498 (1999).
3. Aizenberg, J. Patterned crystallization of calcite in vivo and in vitro. Journal of Crystal Growth 211, 143-148
(2000).
4. Whaley, S. R., English, D. S., Hu, E. L., Barbara, P. F. & Belcher, A. M. Selection of peptides with semiconductor
binding specificity for directed nanocrystal assembly. Nature 405, 665-8 (2000).
5. Weiner, S., Traub, W. & Wagner, H. D. Lamellar bone: structure-function relations. J Struct Biol 126, 241-55
(1999).
6. Hartgerink, J. D., Beniash, E. & Stupp, S. I. Peptide-amphiphile nanofibers: a versatile scaffold for the preparation
of self-assembling materials. Proc Natl Acad Sci U S A 99, 5133-8 (2002).
7. Hartgerink, J. D., Beniash, E. & Stupp, S. I. Self-assembly and mineralization of peptide-amphiphile nanofibers.
Science 294, 1684-8 (2001).
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