Abstract

Self-assembling peptides could be considered a novel class of agents able to harvest an array of micro/nanostructures that are highly attractive in the biomedical field. By modifying their amino acid composition, it is possible to mime several biological functions; when assembled in micro/nanostructures, they can be used for a variety of purposes such as tissue regeneration and engineering or drug delivery to improve drug release and/or stability and to reduce side effects. Other significant advantages of self-assembled peptides involve their biocompatibility and their ability to efficiently target molecular recognition sites. Due to their intrinsic characteristics, self-assembled peptide micro/nanostructures are capable to load both hydrophobic and hydrophilic drugs, and they are suitable to achieve a triggered drug delivery at disease sites by inserting in their structure’s stimuli-responsive moieties. The focus of this review was to summarize the most recent and significant studies on self-assembled peptides with an emphasis on their application in the biomedical field.

Highlights

  • Rahimi-GorjiMolecular self-assembly is a natural process driven by various non-covalent interactions, such as electrostatic and/or hydrophobic, aromatic stacking, hydrogen bonding, or metal coordination interactions [1]

  • Multidomain peptides (MDPs) are a class of self-assembling peptides able to organize themselves in β-sheet motifs, which result in nanofibrous architectures stabilized by a hydrophobic core and hydrogen-bonding networks down the fiber long axis

  • To provide sufficient bioactivity meeting the requirements of clinical applications, Quan et al developed 3D self-assembled hydrogel scaffolds based on bone morphogenetic protein-2 biomimetic peptide (BMPBP), which is a powerful osteoinductive cytokine

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Summary

Introduction

Molecular self-assembly is a natural process driven by various non-covalent interactions, such as electrostatic and/or hydrophobic, aromatic stacking, hydrogen bonding, or metal coordination interactions [1]. The elements of a self-assembling process are macromolecules or their fragments that, under physiological conditions, interact with each another These elements may be equal or different, and their interaction starts from a disordered state leading to a final ordered form (e.g., well-defined crystals or structured macromolecules) [2,3]. Errors in the selfassembly processes can cause serious pathologies, such as neurodegenerative diseases resulting from the abnormal fibrous assemblies of proteins [3,6,7] Considering these physiological roles, in recent years, the self-assembling process has been largely studied; in particular, self-assembling peptides (SAPs) are arousing great attention as novel biomaterials in different fields such as nanomedicine, nanomaterials, and nanobiotechnology [8,9,10,11]. We summarize the most recent and significant studies on SAPs with an emphasis on their application as drugs in the clinical and biomedical field

Self-Assembly Process
Single Amino Acids
Dipeptides
Cyclic Peptides
Stapled Peptides
Amphiphiles and Branched Amphiphilic Peptides
Bolaamphiphilic and Surfactant-Like Peptides
Multi-Domain Peptides
Lipidated Self-Assembly Peptides
Co-Assembly Process
In Diagnostics
In Luminescence and Optoelectronics
For Bioprinting
Self-Assembling Peptides as Drug Delivery Systems
Self-Assembly Peptides for Tissue Engineering and Regenerative Medicine
SAPs in the Pharmaceutical Market
RADA16
PF11 -4
Lanreotide
Findings
Conclusions
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