Self‐Assembled Peptide‐ and Protein‐Based Nanomaterials for Antitumor Photodynamic and Photothermal Therapy

Abbas, Manzar; Zou, Qianli; Li, Shukun; Yan, Xuehai

doi:10.1002/adma.201605021

Cited by 646 publications

(391 citation statements)

References 129 publications

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“…Beyond structure–stability–activity relationship studies, the incorporation of non‐coded amino acids has been exploited in supramolecular chemistry to modulate the conformational propensities of self‐assembling peptides. It has also been used to introduce spectroscopic probes and photosensitizers for diagnostic and therapeutic applications into self‐assembled synthetic peptides (eg, RGD‐based), polypeptides (eg, poly‐Lys/poly‐Leu) and natural proteins (eg, apoferritin) . In particular, the possibility of being able to conjugate photosensitizer moieties (eg, phthalocyanine, protoporphirin, and purpurin) to self‐assembled peptides/proteins, which are able to locally release heat or cytotoxic reactive oxygen species upon controlled light stimulation, has opened new and promising avenues for the fabrication of biocompatible nanostructures for use in antitumor photothermal and photodynamic therapy …”

Section: Discussionmentioning

confidence: 99%

“…At variance, the development of more efficient carbonyl activators and enhancement of automated synthesizers performances made experimentally accessible the manipulation of even long polypeptide chains (50‐90 amino acids) on laboratory routine basis, by inserting any non‐coded amino acid at any protein site for producing large amount of the resulting mutated chain, from milligrams to grams, for studying protein folding, stability, and function . Recently, the efficiency and versatility of SPPS has been extensively exploited to introduce special spectroscopic probes and photosensitizers into self‐assembling peptides for in vivo imaging studies or for the construction of biocompatible supramolecular nanostructures to be used in antitumor photodynamic and photothermal therapy . Furthermore, photo‐inducible chromophores (eg, tris‐bipyridyl stable complexes of ruthenium[II]) have been successfully incorporated at the N‐terminus of alanine‐rich peptides to monitor ultrafast kinetics of helix‐coil conformational transition …”

Section: Introductionmentioning

confidence: 99%

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Protein engineering by chemical methods: Incorporation of nonnatural amino acids as a tool for studying protein folding, stability, and function

et al. 2018

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Proteins are large complex biomolecules that act as the effectors of essentially all cell functions. Due to the intrinsic complexity of protein architecture at the microscopic level and the inadequacy of theoretical methods to predict protein reactivity (ie, folding, stability, and function), protein engineering has emerged as a valuable tool to investigate structure–stability–activity relationships in proteins and nowadays recombinant DNA technologies are the “gold standard” for site‐specifically manipulating a given protein chain. The usefulness of current mutagenesis techniques, however, is limited by the relatively poor chemical diversity of the 20 DNA‐coded amino acids, such that it is difficult to precisely assign the observed change of protein stability or function to the variation of a single physicochemical property at a protein site (ie, hydrophobicity, conformational propensity, polarizability, hydrogen bonding, etc). In this article, we report relevant examples from our laboratory showing that chemical methods, that is, enzyme‐catalyzed semisynthesis and stepwise solid‐phase synthesis, allow to conveniently incorporate non‐natural amino acids with “tailored” side chains into small proteins and thus effectively transfer the structure–activity relationship methodology, typical of the medicinal chemistry approach on small molecules, to the study of folding, stability, and molecular recognition in macromolecular protein systems.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Protein engineering by chemical methods: Incorporation of nonnatural amino acids as a tool for studying protein folding, stability, and function

et al. 2018

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“…Photodynamic Nanoagents Based on Peptide-Modulated Self-Assembly of Photosensitizers PDT, compared with traditional cancer treatment methods, is a minimally invasive and effective method that has been approved by the FDA for some clinical treatments. [32] Our group introduced the cationic diphenylalanine (H-Phe-Phe-NH 2 ·HCl, CDP), which was derived from FF, as a model of an amphiphilic dipeptide for use in combination with another amphiphilic amino acid, 9-fluorenylmethoxycarbonyl-l-lysine (Fmoc-l-Lys). [30] De-excitation then immediately occurs by intersystem crossing to form a triplet state.…”

Section: Nanodrugs Based On Peptide-modulated Self-assembly Of Drugsmentioning

confidence: 99%

Peptide‐Based Supramolecular Nanodrugs as a New Generation of Therapeutic Toolboxes against Cancer

Chang

Zou

Xing

et al. 2019

Advanced Therapeutics

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Peptides are an important class of biomaterials that are widely used in the biomedical field due to their biocompatibility, bioavailability, and structural diversity. They self-assemble into a variety of architectures by weak intermolecular interactions such as π-effects, van der Waals forces, ionic attraction, the hydrophobic effect, and hydrogen bonding, resulting in many advantages in cancer treatment. Self-assembling peptide nanostructures perform two functions: they act as nanocarriers to deliver drugs to tumor sites, and they regulate drug properties, for example, enhancing drug stability, improving the optical properties of photosensitizers, and increasing the immune response. This review focuses on peptide-based supramolecular nanodrugs or nanocarriers for different cancer treatment modalities, such as chemotherapy, phototherapy, and immunotherapy. In particular, peptides with special bioactive properties, such as tumor targeting, microenvironmental responsiveness, and antigenicity, will be highlighted for their utility in the effort to conquer cancer.

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“…They are classified based on number of amino acid conjugates attached to ferrocenyl group and are termed mono‐, di‐, and tri‐peptides. Among them, the behavior of ferrocene‐phenylalanine–phenylalanine (Fc–FF) has been studied in details . Wang and Qi et al reported that Fc–FF changed the conformation of the secondary structures from the flat β‐sheets conformation of phenylalanine–phenylalanine (FF) into twisted β‐sheets, and the detailed diameters of the twists can be controlled by counterions, temperature, and solvents .…”

Section: Introductionmentioning

confidence: 99%

Synthesis and structure analysis of ferrocene‐containing pseudopeptides

et al. 2018

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Ferrocene with its aromaticity and facile redox properties is an attractive moiety to be incorporated into functional moieties. Medicinal applications of ferrocene are well known and ferrocene itself shows cytotoxic and antianemic properties. In this article, we will describe the synthesis and the structure analysis of two pseudopeptides containing a ferrocene moiety as N-terminal group. After purification, Fc-l-Phe-d-Oxd-OBn [l-Phel-phenylalanine; d-Oxd(4R,5S)-4-Methyl-5-carboxy-oxazolidin-2-one] appears as bright brown solid that spontaneously forms brown needles. The X-ray diffraction of the crystals shows the presence of strong π interactions between the ferrocenyl moiety and the phenyl rings, while no NH•••OC hydrogen bonds are formed. This result is confirmed by FT-IR and H NMR analysis. In contrast, both FT-IR and H NMR analysis suggest that Fc-(l-Phe-d-Oxd) -OBn forms a turn conformation stabilized by intramolecular NH•••OC hydrogen bonds in solution. Chiroptical spectroscopies (ECD and VCD) substantially confirmed the absence of a well-defined folded structure. The presence of the Fc moiety is responsible for specific ECD signals, one of which displayed pronounced temperature dependence and is directly related with the helicity assumed by the Fc core. Solid-state ECD spectra were recorded and rationalized on the basis of the X-ray geometry and quantum-mechanical calculations.

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Self‐Assembled Peptide‐ and Protein‐Based Nanomaterials for Antitumor Photodynamic and Photothermal Therapy

Cited by 646 publications

References 129 publications

Protein engineering by chemical methods: Incorporation of nonnatural amino acids as a tool for studying protein folding, stability, and function

Protein engineering by chemical methods: Incorporation of nonnatural amino acids as a tool for studying protein folding, stability, and function

Peptide‐Based Supramolecular Nanodrugs as a New Generation of Therapeutic Toolboxes against Cancer

Synthesis and structure analysis of ferrocene‐containing pseudopeptides

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