Gerbelli, Barbara B.
Vassiliades, Sandra V.
Rojas, Jose E. U.
Pelin, Juliane N. B. D.
Mancini, Rodrigo S. N.
Pereira, Wallace S. G.
Aguilar, Andrea M.
Alves, Wendel A.
Total Authors: 11
 Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210580 Santo Andre - Brazil
 Univ Fed Sao Paulo, Inst Ciencias Ambientais Quim & Farmaceut, BR-09972270 Diadema - Brazil
 Univ Roma Tor Vergata, Dept Chem Sci & Technol, Via Cracovia 50, I-00133 Rome, RM - Italy
 Liverpool John Moores Univ, Sch Pharm & Biomol Sci, Byrom St, Liverpool L3 3AF, Merseyside - England
Total Affiliations: 5
MACROMOLECULAR CHEMISTRY AND PHYSICS;
n. 14, SI
Web of Science Citations:
Self-assembled structures obtained from organic molecules have shown great potential for applications in a wide range of domains. In this context, short peptides prove to be a particularly versatile class of organic building blocks for self-assembled materials. These species afford the biocompatibility and polymorphic richness typical of proteins while allowing synthetic availability and robustness typical of smaller molecules. At the nano-to-mesoscale, the architectures obtained from peptide units exhibit stability and a large variety of morphologies, the most common of which are nanotubes, nanoribbons, and nanowires. This review describes the formation of peptide-based self-assembled structures triggered by different stimuli (e.g., ionic strength, pH, and polarity), and the interactions that drive the assembling processes. It is surveyed how judicious molecular design is exploited to impart favourable assembling properties to afford systems with desired characteristics. A large body of literature provides the experimental and in silico data to predict self-assembly in a given peptide system and obtain different supramolecular organizations for applications in a wide range of fields, from transport to sensing, from catalysis to drug delivery and tissue regeneration. (AU)