From structure to application: Progress and opportunities in peptide materials development

Lopez-Silva, Tania L.

doi:10.1016/j.cbpa.2021.06.006

Cited by 21 publications

(15 citation statements)

References 130 publications

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“…Self-assembled peptide material has important biomedical applications ( 1 ). To enable rational design of peptide material requires a deep understanding of the chemical and physicochemical rules guiding peptide assemblies and folding.…”

Section: Discussionmentioning

confidence: 99%

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Atomic structure of Lanreotide nanotubes revealed by cryo-EM

Pieri

Wang

Arteni

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

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Functional and versatile nano- and microassemblies formed by biological molecules are found at all levels of life, from cell organelles to full organisms. Understanding the chemical and physicochemical determinants guiding the formation of these assemblies is crucial not only to understand the biological processes they carry out but also to mimic nature. Among the synthetic peptides forming well-defined nanostructures, the octapeptide Lanreotide has been considered one of the best characterized, in terms of both the atomic structure and its self-assembly process. In the present work, we determined the atomic structure of Lanreotide nanotubes at 2.5-Å resolution by cryoelectron microscopy (cryo-EM). Surprisingly, the asymmetric unit in the nanotube contains eight copies of the peptide, forming two tetramers. There are thus eight different environments for the peptide, and eight different conformations in the nanotube. The structure built from the cryo-EM map is strikingly different from the molecular model, largely based on X-ray fiber diffraction, proposed 20 y ago. Comparison of the nanotube with a crystal structure at 0.83-Å resolution of a Lanreotide derivative highlights the polymorphism for this peptide family. This work shows once again that higher-order assemblies formed by even well-characterized small peptides are very difficult to predict.

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Section: Discussionmentioning

confidence: 99%

“…Peptide assemblies forming hydrogels or fibrils have been used for biomedical applications, such as drug delivery, cell culture, vaccines, and tissue regeneration ( 1 ). Peptides are indeed potentially important molecules as drugs, but they are generally very sensitive to enzymatic degradation in vivo.…”

mentioning

confidence: 99%

Atomic structure of Lanreotide nanotubes revealed by cryo-EM

Pieri

Wang

Arteni

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

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“…Peptides are usually defined as the biomacromolecules that contain less than 50 amino acids linked by peptide bonds, with the intrinsic characteristics of folding and bioactivities like recognition and response. Since the emergences of technologies for the peptide manufacture and screening, especially the solid-phase peptide synthesis proposed by Merrifield in 1963(Merrifield, 1963 and the phage display described by Smith in 1985(Smith, 1985, numerous peptide-based pharmaceuticals and functional materials have been developed (Figure 1A) (Hosoyama et al, 2019;Lopez-Silva and Schneider, 2021;Muttenthaler et al, 2021). Particularly, self-assembling peptides have attracted increasing interest due to their improved stability and biological performance (Guyon et al, 2018;Levin et al, 2020), and have been applied in a wide range of fields including the tissue engineering (Gelain et al, 2020;Zhang et al, 2021), drug delivery (Moitra et al, 2014;Abbas et al, 2017;Yang J. et al, 2020;Kumar et al, 2020;, catalysis (Rufo et al, 2014;Wang M. et al, 2020;Liu Q. et al, 2021;Chen et al, 2021), semi-conducting device (Tao et al, 2017), and energy materials (Hu et al, 2018;Lee et al, 2018;Nguyen et al, 2021).…”

Section: Self-assembling Peptidementioning

confidence: 99%

Mitochondria-Targeted Self-Assembly of Peptide-Based Nanomaterials

Luo

Gao

Duan

et al. 2021

Front. Bioeng. Biotechnol.

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Mitochondria are well known to serve as the powerhouse for cells and also the initiator for some vital signaling pathways. A variety of diseases are discovered to be associated with the abnormalities of mitochondria, including cancers. Thus, targeting mitochondria and their metabolisms are recognized to be promising for cancer therapy. In recent years, great efforts have been devoted to developing mitochondria-targeted pharmaceuticals, including small molecular drugs, peptides, proteins, and genes, with several molecular drugs and peptides enrolled in clinical trials. Along with the advances of nanotechnology, self-assembled peptide-nanomaterials that integrate the biomarker-targeting, stimuli-response, self-assembly, and therapeutic effect, have been attracted increasing interest in the fields of biotechnology and nanomedicine. Particularly, in situ mitochondria-targeted self-assembling peptides that can assemble on the surface or inside mitochondria have opened another dimension for the mitochondria-targeted cancer therapy. Here, we highlight the recent progress of mitochondria-targeted peptide-nanomaterials, especially those in situ self-assembly systems in mitochondria, and their applications in cancer treatments.

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“…Beyond lipid nanoparticles, which have gained much recent attention for their roles in mRNA based COVID-19 vaccines, peptides have emerged as promising nanoscale delivery systems in recent years. Peptide-based materials benefit from chemical versatility, tunable amphiphilicity, reduced barriers to eventual approval by the FDA, and a body of work demonstrating their promise as designable delivery vehicles. − …”

Section: Introductionmentioning

confidence: 99%

Encapsulation of Gold-Based Anticancer Agents in Protease-Degradable Peptide Nanofilaments Enhances Their Potency

et al. 2022

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We investigated the use of amphiphilic, protease-cleavable peptides as encapsulation moieties for hydrophobic metallodrugs, in order to enhance their bioavailability and consequent activity. Two hydrophobic, gold-containing anticancer agents varying in aromatic ligand distribution (Au(I)-N-heterocyclic carbene compounds 1 and 2) were investigated. These were encapsulated into amphiphilic decapeptides that form soluble filamentous structures with hydrophobic cores, varying supramolecular packing arrangements and surface charge. Peptide sequence strongly dictates the supramolecular packing within the aromatic core, which in turn dictates drug loading. Anionic peptide filaments can effectively load 1, and to a lesser extent 2, while their cationic counterparts could not, collectively demonstrating that loading efficiency is dictated by both aromatic and electrostatic (mis)matching between drug and peptide. Peptide nanofilaments were nontoxic to cancerous and noncancerous cells. By contrast, those loaded with 1 and 2 displayed enhanced cytotoxicity in comparison to 1 and 2 alone, when exposed to Caki-1 and MDA-MB-231 cancerous cell lines, while no cytotoxicity was observed in noncancerous lung fibroblasts, IMR-90. We propose that the enhanced in vitro activity results from the enhanced proteolytic activity in the vicinity of the cancer cells, thereby breaking the filaments into drug-bound peptide fragments that are taken up by these cells, resulting in enhanced cytotoxicity toward cancer cells.

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From structure to application: Progress and opportunities in peptide materials development

Cited by 21 publications

References 130 publications

Atomic structure of Lanreotide nanotubes revealed by cryo-EM

Atomic structure of Lanreotide nanotubes revealed by cryo-EM

Mitochondria-Targeted Self-Assembly of Peptide-Based Nanomaterials

Encapsulation of Gold-Based Anticancer Agents in Protease-Degradable Peptide Nanofilaments Enhances Their Potency

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