2022
DOI: 10.1016/j.mtbio.2022.100337
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Structural control of self-assembled peptide nanostructures to develop peptide vesicles for photodynamic therapy of cancer

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Cited by 9 publications
(10 citation statements)
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“…[3] More specifically, they exhibit unique attributes such as hydrogen bonding potential, inherent chirality from amino acids, polymorphism [4] and conformational rigidity stemming from peptide bonds. [3] Furthermore, peptides can be derived naturally or synthetically, and examples include recombinant hormones, antimicrobial peptides, antibodies, and recombinant enzymes, [5] in addition to the possibilities for incorporating nonnatural amino acids to diversify the chemistry further. [6] Despite significant advancements in drug development, there are still many barriers for precision medicine.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…[3] More specifically, they exhibit unique attributes such as hydrogen bonding potential, inherent chirality from amino acids, polymorphism [4] and conformational rigidity stemming from peptide bonds. [3] Furthermore, peptides can be derived naturally or synthetically, and examples include recombinant hormones, antimicrobial peptides, antibodies, and recombinant enzymes, [5] in addition to the possibilities for incorporating nonnatural amino acids to diversify the chemistry further. [6] Despite significant advancements in drug development, there are still many barriers for precision medicine.…”
Section: Introductionmentioning
confidence: 99%
“…About 10 % of the drugs in the pharmaceutical market are peptide or protein drugs including 485 entries for peptide drugs in DrugBank [2] and 239 entries in THPdb of FDA‐approved peptide drugs [1] . Peptide and protein drugs have significant potential in diverse applications, ranging from sensing and catalysis to therapeutics due to their biocompatibility, flexibility in design through amino acid sequence variations, and unique molecular topologies [3] . More specifically, they exhibit unique attributes such as hydrogen bonding potential, inherent chirality from amino acids, polymorphism [4] and conformational rigidity stemming from peptide bonds [3] .…”
Section: Introductionmentioning
confidence: 99%
“…23 In the last two decades, a plethora of studies on molecular self-assembly have led to a deeper understanding of the basic principles and established the relationship between the structure and function of self-assembled systems. In situ selfassembly based on peptides has been widely discussed, [24][25][26][27] but this method is not limited to peptides, as other nanomaterials such as polymers, 28 small molecule prodrugs, 29 inorganic metals, 30 and nucleic acids 31,32 can also self-assemble. In this review, we discuss the principles of self-assembly of various nanomaterials in different microenvironments in the body, their applications, and the advantages of in situ self-assembly in drug delivery and disease diagnosis and treatment.…”
Section: Introductionmentioning
confidence: 99%
“…It has been demonstrated that self-assembled peptides with nanostructures have greater stability and performance, as well as enthralling biological effects, in comparison to standard self-assembled peptides. The main route of cellular uptake of these peptide-based nanostructures is through endocytosis, but it is severely affected by enzymatic degradation and lysosomal entrapment. , When the nanoparticle’s surface was modified with peptides, they successfully assisted the nanoparticles in intracellular escape. Dipeptides with small molecular weight (Try-Phe) can be used to synthesize dipeptide nanoparticles, which can be self-assembled through ion chelation reactions (Zinc ion chelation reactions) .…”
Section: Introductionmentioning
confidence: 99%