Drug Delivery Applications of Peptide Materials

Abstract

Peptides play an essential role in biotechnological applications as therapeutic and diagnostic agents due to their tunable activity for desired function. So far, a variety of peptide therapeutics and their peptide-based carriers have been engineered for drug delivery applications. However, in order to design and develop such systems for tissue-specific applications, the cellular microenvironment must be properly considered. Peptide-based materials have vast potential applications, particularly for cancer-related systems. Thus, in this chapter, we first focus on different design strategies and considerations for drug-release mechanisms in peptide-based materials. Then, we explain how tumor microenvironments may be distinguished from healthy tissue, including discussion of tumor-specific drug delivery strategies. Finally, the growing significance of peptide chemotherapeutics will be emphasized in terms of design concerns and current applications.

Peptide Aggregation Induced Immunogenic Rupture (PAIIR)

“…Engineering the fine‐tuned cellular aggregation of peptides requires well‐characterized intermolecular interactions. [ 27 , 28 ] Understanding these interactions allows the rational design of peptides to encompass desired properties, such as aggregation on the cell that induces stress for inducing ICD and cell membrane rupturing for DAMP release. We utilized the CoOP strategy to design peptides with strong enough affinity to aggregate in the cellular environment.…”

“…Interest in peptide‐based materials has flourished in health, energy, materials science, and national security. [ 27 ] By advancing the discovery of peptide domains with unique intermolecular interactions, the design of peptides with desired properties in appropriate conditions can be achievable. Inspired by the mechanism of natural membrane rupturing proteins that aggregate and induce ICD, in this study, we designed a new peptide‐based tool, [II], via the CoOP strategy.…”

Peptide framework for screening the effects of amino acids on assembly

“…In particular, self-assembly into fibrillar peptide aggregates is abundant in nature and various synthetic technologies in biomedical research (2)(3)(4)(5)(6)(7)(8)(9) and materials science (10)(11)(12). The organization of peptide assemblies emerges from small changes in the amino acid sequence that provides noncovalent interactions, such as electrostatic forces, hydrogen bonds, hydrophobic effects, and aromatic stacking (13,14). Understanding the effects of these small changes is essential to identify the structure-property relation and create small peptides that do not simply mimic natural sequences but instead are rationally designed for the desired properties.…”

Temperature-Responsive Nano-Biomaterials from Genetically Encoded Farnesylated Disordered Proteins

“…The development of new protein-based biopharmaceuticals and materials is a vibrant area of research at the interface of chemistry, biology, and materials science and engineering. − Efforts in this space have traditionally focused on engineering the amino acid sequence and structure of proteins to achieve a specific function for applications including biomaterials, − sensors, and biocatalysts, among others. − Instead of changing the sequence of proteins, cells leverage an alternative strategy, post-translational modification (PTMs), to modulate a protein’s structure and function with exquisite spatiotemporal control . Despite the significant interest in the biology of PTMs, this strategy remains underutilized for diversifying physicochemical properties, engineering capabilities, and the biological behavior of proteins. − This lacuna exists because the synthesis of proteins with compositionally defined PTM patterns remains challenging, and although more than 300 PTMs have been identified, the energetic interplay and (bio)­material consequences of only a handful of these modifications have been systematically studied …”