Peptide-based Synthetic Design, Construction and Morphology of Soft Structures

Abstract

Peptide-based self-assembly offers a unique entry into the construction of soft structures with interesting material properties and functions. Aromatic amino acid-containing peptides are commonly employed as they exhibit high propensity to aggregate due to increased hydrophobic content, promotion of favorable secondary structures, planarity and the possibility of π-π interactions. Incorporation of covalent scaffolds, stimuli-responsive handles and carbohydrate moieties augment beneficial characteristics to the resulting peptide conjugates. These modifications were shown to enforce self-association, elicit stimuli response and achieve improved hydrophilic properties, to name but a few.

Phase Transition and Crystallization Kinetics of a Supramolecular System in a Microfluidic Platform

“…In nature, functional and complex biological nanostructures are formed by the self-assembly of a wide range of biomolecules, including proteins, nucleic acids, and lipids, providing the fundamental cellular machinery. Inspired by this phenomenon, extensive efforts have been made to exploit the naturally evolved principles governing self-assembly to design artificial materials with tailored functions and properties. , Supramolecular self-assembly of short peptides and modified amino acids is a key subsection in the field of materials science, facilitating the development and fabrication of novel nanomaterials. − Such nanomaterials are produced through spontaneous “bottom-up” self-assembly, where stabilizing noncovalent interactions lead to a diverse set of architectures, such as spheres, tubes, fibers, vesicles, and toroids. − Through their self-assembly into fibrillar networks, short peptides, and amino acids can also form three-dimensional (3D) hydrogels, which have been shown to support cell growth and proliferation. Accordingly, such peptide-based hydrogels have recently been employed for tissue engineering, , regenerative medicine, and as drug delivery platforms. , In the past decade, diphenylalanine (Phe-Phe) and other aromatic biomolecules, such as tert -butoxycarbonyl-diphenylalanine (Boc-Phe-Phe), Fmoc-Phe, Fmoc-Phe-Phe, and Fmoc-dihydroxyphenylalanine (Fmoc-DOPA), have been extensively explored and shown to serve as promising candidates for a wide range of applications, − such as metal–organic frameworks, super-hydrophobic surfaces, and energy storage devices .…”

Constitutionally Isomeric Aromatic Tripeptides: Self‐Assembly and Metal‐Ion‐Modulated Transformations

“…The hydrogen‐bonding moieties‐peptide bonds, N‐ and C‐termini‐together with aromatic groups are an attractive combination. Therefore, aromatic di or tripeptide conjugates are much popular which facilitates the persistent supramolecular association that provides self‐assembled structures of high stability . A simple diphenylalanine short peptide, a core recognition motif of Amyloid β‐peptide which was identified through a systemic reductionist methodology (Scheme ), was found sufficient to create wide variety of nanostructures for wider applications by number of scientific reports …”

Soft structure formation and cancer cell transport mechanisms of a folic acid–dipeptide conjugate

“…Given our ongoing interest in peptide soft structures and bionanoconjugation based on guanine tetrad formation , we decided to investigate whether bottom‐up approach with FA‐containing peptide building blocks will reveal interesting structural features and delivery properties. The design of FA conjugates could be achieved via two different routes: first, by making FA‐conjugated peptides, followed by their self‐assembly, or through postsynthetic modification of in situ assembled peptide nanotubes by FA (Scheme ) .…”