Cell-penetrating peptides (CPP) provide an efficient strategy for the intracellular delivery of bioactive molecules in various biomedical applications. This review focuses on recent advances in the use of CPPs to deliver anticancer therapeutics and imaging reagents to cancer cells, along with CPP contributions to novel tumor-targeting techniques. CPPs are now used extensively to deliver a variety of therapeutics, despite lacking cell specificity and having a short duration of action. Resolution of these shortcomings to enable increased cancer cell and/or tumor specificity could improve CPP-based drug delivery strategies, expand combined drug delivery possibilities, and strengthen future clinical applications of these peptides.
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http://dx.doi.org/10.1016/j.molmed.2015.06.005 | DOI Listing |
Expert Opin Drug Deliv
January 2025
Center for Targeted Drug Delivery, Department of Biomedical and Pharmaceutical Sciences, Chapman University School of Pharmacy, Irvine, California, USA.
Introduction: Cyclic antimicrobial peptides (CAMPs) are gaining attention as promising candidates in advanced drug delivery systems due to their structural stability, resistance to proteolytic degradation, and versatile therapeutic potential. Their unique properties enable applications that extend beyond combating multidrug-resistant (MDR) pathogens. Their amphipathic and cell-penetrating properties allow them to efficiently transport drugs across cellular membranes.
View Article and Find Full Text PDFSci Rep
January 2025
The Comprehensive Cancer Center, Nanjing Drum Tower Hospital, Affiliated Hospital of Medical School, Nanjing University and Clinical Cancer Institute of Nanjing University, Nanjing, 210008, China.
Cell-penetrating peptides (CPPs) have been shown to have superior material transport ability because poor infiltration of activated lymphocytes into tumors is one of the crucial factors limiting the therapeutic effect of tumor immunotherapy. Numerous studies have investigated the potential application of CPPs in tumor immunotherapy. This review delves into the crucial role that CPPs play in enhancing tumor immunotherapy, emphasizing their impact on various immunotherapy strategies, such as cytokine therapy, adoptive cell therapy, cancer vaccines, and immune checkpoint inhibitors.
View Article and Find Full Text PDFPeptides play critical roles in cellular functions such as signaling and immune regulation, and peptide-based biotherapeutics show great promise for treating various diseases. Among these, cell-penetrating peptides (CPPs) are particularly valuable for drug delivery due to their ability to cross cell membranes. However, the mechanisms underlying CPP-mediated transport, especially across the blood-brain barrier (BBB), remain poorly understood.
View Article and Find Full Text PDFACS Cent Sci
January 2025
Centre for Inflammation Research, The University of Edinburgh, EH16 4UU Edinburgh, U.K.
The cellular uptake routes of peptides and proteins are complex and diverse, often handicapping therapeutic success. Understanding their mechanisms of internalization requires chemical derivatization with approaches that are compatible with wash-free and real-time imaging. In this work, we developed a new late-stage labeling strategy for unprotected peptides and proteins, which retains their biological activity while enabling live-cell imaging of uptake and intracellular trafficking.
View Article and Find Full Text PDFAmino Acids
January 2025
Tissue Engineering and Regenerative Medicine Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran.
In recent years, the use of cationic peptides as alternative drugs with anticancer activity has received attention. In this study, the targeted release of curcumin (Cur) and CM11 peptide alone and together against hepatocellular carcinoma (HCC) was evaluated using chitosan nanoparticles (CS NPs) coated with Pres1 that target the SB3 antigen of HCC cells (PreS1-Cur-CM11-CS NPs). SB3 protein is the specific antigen of HCC and the PreS1 peptide is a part of the hepatitis B antigen, which can specifically bind to the SB3 protein.
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