Heterochiral peptide self-assembly and nanomaterials

Short peptides (especially di- and tripeptides) are attractive building blocks for nanostructures and supramolecular materials, due to their simplicity and ease of preparation.1,2 Besides, tripeptides are also minimalist motifs capable of delivering a biological message to cells (e.g., RGD for cell adhesion).3

There are several approaches to drive self-assembly of short peptides. In particular, a relatively unexplored avenue is the use of chirality (i.e., appropriate choice of D- versus L-amino acids) to fine-tune the supramolecular behaviour of tripeptides and their ordered self-assembly into nanostructured materials. Recently, a few examples of hydrophobic tripeptides bearing D-amino acid(s) at selected positions have been reported to rapidly form nanostructured hydrogels under physiological conditions at which their homochiral stereoisomers (e.g., L-tripeptides) do not.4-7 This unexpected behaviour raises interesting questions that go beyond peptide self-assembly, including the transfer of chirality from simple molecules to supramolecular nanoarchitectures, and how these interact with life. Current investigations tackle:

- de novo design of self-assembling short peptides

- transfer of chirality from heterochiral tripeptides to supramolecular architectures

- preparation of hybrid or nanocomposite materials bearing different chemical components (e.g., peptides, carbon nanomaterials, inorganic nanoparticles, drugs, etc.) for added properties

- design of smart functional nanostructured materials (e.g., that respond to light, magnetic guidance, electric fields, etc.) for biological use (e.g., cell culture, tissue engineering, drug delivery)



1. Nat. Chem. 2015, 7, 30.

2. Mol. Biosci. 2011, 11, 160.

3. J. Med. Chem. 2011, 54, 1111.

4. Chem. Commun. 2012, 48, 2195.

5. Nanoscale 2012, 4, 6752.

6. Nanoscale 2014, 6, 5172.

7. J. Mater. Chem. B 2015, 3, 8123.


Research Group

Marchesan Group
Last update: 09-27-2021 - 19:50