Peptides as Diagnostic, Therapeutic, and Theranostic Tools: Progress and Future Challenges

Thakur, Reena; Suri, C. Raman; Kaur, Indu Pal; Rishi, Praveen

doi:10.1615/critrevtherdrugcarriersyst.2022040322

Cited by 10 publications

(3 citation statements)

References 216 publications

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“…There are non-self-assembling therapeutic peptides that can deliver immunomodulatory agents. Such therapeutic peptides have been thoroughly reviewed and will not be discussed here (Lau and Dunn, 2018;Li et al, 2021;Thakur et al, 2022).…”

Section: Binding Domainsmentioning

confidence: 99%

Self-assembling peptides as immunomodulatory biomaterials

Hernández

Hartgerink²,

Young³

2023

Front. Bioeng. Biotechnol.

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Self-assembling peptides are a type of biomaterial rapidly emerging in the fields of biomedicine and material sciences due to their promise in biocompatibility and effectiveness at controlled release. These self-assembling peptides can form diverse nanostructures in response to molecular interactions, making them versatile materials. Once assembled, the peptides can mimic biological functions and provide a combinatorial delivery of therapeutics such as cytokines and drugs. These self-assembling peptides are showing success in biomedical settings yet face unique challenges that must be addressed to be widely applied in the clinic. Herein, we describe self-assembling peptides’ characteristics and current applications in immunomodulatory therapeutics.

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Section: Binding Domainsmentioning

confidence: 99%

Self-assembling peptides as immunomodulatory biomaterials

Hernández

Hartgerink²,

Young³

2023

Front. Bioeng. Biotechnol.

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“…Peptides, due to their diverse properties, find multifaceted applications, ranging from pivotal roles in pharmaceuticals to essential functions in cosmetic chemistry, diagnostics, and biomaterials. [1][2][3][4][5][6] The burgeoning interest in peptides has intensified in recent years, as advancements in both biological and chemical manufacturing methods have rendered their production increasingly accessible. 7,8 Traditional approaches to obtaining pure peptides have relied on solid-phase peptide synthesis (SPPS) and reversed-phase high-pressure liquid chromatography (RP-HPLC).…”

Section: Introductionmentioning

confidence: 99%

Optimization of peptide synthesis time and sustainability using novel eco‐friendly binary solvent systems with induction heating on an automated peptide synthesizer

Pacini,

Muthyala,

Aguiar

et al. 2024

Journal of Peptide Science

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On December 12th, 2023, the European Commission took regulatory action to amend Annex XVII of REACH, imposing restrictions on the use of N,N‐dimethylformamide (DMF) within the EU market owing to its high toxicity. Historically, DMF has been widely considered the gold standard for solid‐phase peptide synthesis (SPPS). Being urgent to propose alternative solvents, we tested the suitability of non‐hazardous neat and mixed solvents. Notably, binary solvent mixtures containing dimethyl sulfoxide as one of the solvent partners demonstrated high efficacy in solubilizing reagents while maintaining the desired swelling characteristics of common resins. A series of binary solvent mixtures were tested in automated SPPS, both at room temperature and high temperature, employing the PurePep® Chorus synthesizer, which enabled controlled induction heating between 25 and 90°C with oscillation mixing. The performances were assessed in challenging peptide sequences, i.e., ACP (65–74), and in longer and aggregating sequences like SARS‐CoV‐2 RBM (436–507) and β‐amyloid (1–42). Furthermore, as part of the proposed sustainable approach to minimize the utilization of hazardous solvents, we coupled the novel PurePep EasyClean catch‐and‐release purification technology. This work, addressing regulatory compliance, emphasizes the crucial role of green chemistry in advancing safer and more environmentally friendly practices in SPPS.

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“…This receptor‐dependent endocytosis can boost the absorption of drugs in the cell, resulting in greater therapeutic effectiveness (Figure 2 ). 28 , 29 , 30 , 31 This is especially effective for delivering drugs with low cell permeability or that breakdown quickly in the extracellular environment. RGD‐functionalized drug carriers can be engineered to carry numerous therapeutic agents to the target area, such as chemotherapeutic medicines and genes.…”

Section: Introductionmentioning

confidence: 99%

RGD peptide in cancer targeting: Benefits, challenges, solutions, and possible integrin–RGD interactions

Javid,

Oryani,

Rezagholinejad

et al. 2024

Cancer Medicine

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RGD peptide can be found in cell adhesion and signaling proteins, such as fibronectin, vitronectin, and fibrinogen. RGD peptides' principal function is to facilitate cell adhesion by interacting with integrin receptors on the cell surface. They have been intensively researched for use in biotechnology and medicine, including incorporation into biomaterials, conjugation to medicinal molecules or nanoparticles, and labeling with imaging agents. RGD peptides can be utilized to specifically target cancer cells and the tumor vasculature by engaging with these integrins, improving drug delivery efficiency and minimizing adverse effects on healthy tissues. RGD‐functionalized drug carriers are a viable option for cancer therapy as this focused approach has demonstrated promise in the future. Writing a review on the RGD peptide can significantly influence how drugs are developed in the future by improving our understanding of the peptide, finding knowledge gaps, fostering innovation, and making drug design easier.

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Peptides as Diagnostic, Therapeutic, and Theranostic Tools: Progress and Future Challenges

Cited by 10 publications

References 216 publications

Self-assembling peptides as immunomodulatory biomaterials

Self-assembling peptides as immunomodulatory biomaterials

Optimization of peptide synthesis time and sustainability using novel eco‐friendly binary solvent systems with induction heating on an automated peptide synthesizer

RGD peptide in cancer targeting: Benefits, challenges, solutions, and possible integrin–RGD interactions

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