Abstract
The essence of modern nanotechnology is manifested in the formation of well-ordered nanostructures by a process of self-association. Peptides are among the most useful building blocks for organic bionanostructures such as nanotubes, nanospheres, nanotapes, nanofibrils, and other different ordered structures at the nanoscale. Peptides are biocompatible, chemically diverse, and much more stable and can be readily synthesized on a large scale. Also, they have diverse application in biosensors, tissue engineering, drug delivery, etc. Here, we report a short cystine-based dipeptide, which spontaneously self-associates to form straight, unbranched nanotubes. Such self-assembled nanobiomaterials provide a novel possibility of designing new functional biomaterials with potential applications in nanobiotechnology. The formation of nanotubes in solution state has been demonstrated by atomic force microscopy and scanning electron microscopy. Infrared absorption and circular dichroism demonstrated the intermolecular β-sheet-like backbone hydrogen bonding in juxtaposing and stacking of aromatic side chains.
Highlights
There has been rapid advancement in the development of self-assembled nanobiomaterials, such as nanotubes, nanocrystals, and nanowires, which have potential application in electronics, biosensors, catalysis, drug delivery, and tissue engineering [1,2,3,4]
Synthesis of the dipeptide The dipeptide was synthesized by conventional solutionphase methodology (Scheme 1)
This study clearly demonstrates that short water-soluble benzylcystine dipeptide self-assembles to form a supramolecular extended structure with β-sheet-like intermolecular hydrogen-bonding pattern in solid state, and this dipeptide forms an ordered nanostructure from an aqueous solution under the proper conditions
Summary
There has been rapid advancement in the development of self-assembled nanobiomaterials, such as nanotubes, nanocrystals, and nanowires, which have potential application in electronics, biosensors, catalysis, drug delivery, and tissue engineering [1,2,3,4]. There are various designing rules of the synthesis of these biomaterials, where secondary structure of the self-assembled fiber, the thickness of fiber, and hydrogel porosity, and different mechanical properties can all be varied predictably by changing the amino acid sequence, its concentration, the surrounding media, and its processing route [6,7,8]. It has been already reported that cyclic peptides, amphiphilic peptides, and amyloid-inspired peptides can form ordered nanostructures with different morphologies including nanowires, nanotubes, nanovesicles, nanofibrils, and nanosheets [12,13,14].
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