Peptides short, assembly

Cejas MA, Kinney WA, Chen C, Leo GC, Tounge BA, Vinter JG, Joshi PP, Maryanoff BE. Collagen-related peptides self-assembly of short, single strands into a functional biomaterial of micrometer scale. J Am Chem Soc 2007 129 2202-2203. 

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. 

As discussed in Section IV, photolysis is a mild cleavage method that is attractive for combinatorial drug discovery because products can be released into neutral aqueous solution suitable for direct screening. Amine analogues of the hydroxyl resins described earlier have been reported. Thus, (aminomethyl)-6>-nitrobenzyl supports 7n have been reported on which short peptide amides could be synthesized with cleavage occurring upon irradiation at 350 nm in the presence of ammonia [323]. 2-Nitrobenzhydryl (NBHA) supports 7o have also been used for peptide amide assembly using Boc-protected amino acids. The anchor was unaffected by 4 N HCl-dioxane... 

Gilead, S., and Gazit, E. (2005). Self-organization of short peptide fragments From amyloid fibrils to nanoscale supramolecular assemblies. Supramol. Chem. 17, 87-92. 

Similarly, iterative NRPSs operate in a linear fashion but utilize at least one domain or module multiple times for the synthesis of a single NRP product. Thus, peptides assembled by iterative synthetases contain short, repeating units of peptide building blocks. In such systems, the terminal PCP-TE (or infrequendy PCP-C) didomain is responsible for both condensation of the repeating peptide units and chain release from the assembly line. NRPs biosynthesized in this manner include enniatin, enterobactin, bacillibactin, " gramicidin and the depsi-peptides valinomycin and cereulide. Of these examples, condensation of the precursor peptides for both enterobactin and gramicidin S has been extensively studied and will be discussed in detail. 

Bose PP, Drew MGB, Baneijee A. Nanoparticles on self-assembling pseudopeptide-based nanofiber by using a short peptide as capping agent for metal nanoparticles. Org Lett 2007 9 2489-2492. 

Ray S, Das AK, Drew MGB, Baneqee A. A short water-soluble self-assembling peptide forms amyloid-like fibrils. Chem Commun 2006 40 4230-4232. 

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