Self-assembled molecules peptides

Figure 14.10 Self-assembly of peptide-amphiphiles into nanofibers (a) a peptide amphi-phile molecule with five distinct regions designed for hydroxyapatite mineralization, (b) a schematic of molecular self-assembly, and (c) a negatively stain transmission electron microscopy image of the nanofibers. Reprinted from Hartgerink et al. (2001). Copyright 2001 American Association for the Advancement of Science.

The following papers focus mainly on various aspects associated with the self-assembly of peptides. Peptides are relatively short sequences of amino acids, typically less than 50. The limited number of residues brings simplicity but still allows for sufficient differentiation to study self-assembly in its various details. The compositional freedom of the primary molecule allows for a sufficiently rich hierarchical structure creation through aggregation of individual peptides into supramolecular constructs resulting in interesting materials. This chapter looks into relevant patent literature as a reflection of the state of the art of technology in peptide self-assembly. 

Fig. 5.20 a Model of compound 75-3a in its all-Zran conformation (front view), b a supramolecular column (lateral view) by self-assemble of peptide molecules into a helical organization in a helical fashion, and c a possible lattice (the arrows indicate the direction of the dipole moment). Reproduced from Ref. [100] by permission of John Wiley Sons Ltd... 

Cui Honggang, Webber J. Matthew, and Stuppl. Samuel. Self-assembly of peptide amphiphiles From molecules to nanostructures to biomaterials. Biopolymers. 94 no. 1 (2010) 1-18. 

Fig. 3. (a) Chemical stmcture of a synthetic cycHc peptide composed of an alternating sequence of D- and L-amino acids. The side chains of the amino acids have been chosen such that the peripheral functional groups of the dat rings are hydrophobic and allow insertion into Hpid bilayers, (b) Proposed stmcture of a self-assembled transmembrane pore comprised of hydrogen bonded cycHc peptides. The channel is stabilized by hydrogen bonds between the peptide backbones of the individual molecules. These synthetic pores have been demonstrated to form ion channels in Hpid bilayers (71). 

Self-Assembling Peptides as Frameworks for Other Functional Molecules. 46... 

If attachment of a particular constituent is incompatible with peptide synthesis, or detrimental to self-assembly, an alternative approach would be to add a functional group that selectively binds this molecule. After synthesis and self-assembly of the peptide, the difficult molecule could be introduced to the binding site included on the peptide. 

Niece KL, Hartgerink JD, Donners J et al (2003) Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. J Am Chem Soc 125 7146-7147... 

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