Cell-Penetrating Peptides (CPPs) as Therapeutic and Diagnostic Agents for Cancer

被引:43
作者
Bottens, Ryan A. [1 ]
Yamada, Tohru [1 ,2 ]
机构
[1] Univ Illinois, Coll Med, Dept Surg, Div Surg Oncol, Chicago, IL 60612 USA
[2] Univ Illinois, Coll Med & Engn, Richard & Loan Hill Dept Biomed Engn, Chicago, IL 60607 USA
关键词
cell penetration; protein transduction; targeted delivery; therapeutics; diagnostics; clinical trial; REDOX PROTEIN AZURIN; INTELLIGENT BIOSYNTHETIC NANOBIOMATERIALS; ARGININE-RICH PEPTIDES; DELIVERY IN-VITRO; DRUG-DELIVERY; P53; UBIQUITINATION; BREAST-CANCER; P-28; NANOPARTICLES; TRANSLOCATION;
D O I
10.3390/cancers14225546
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Cell-Penetrating Peptides (CPPs) are short peptides consisting of <30 amino acids. Their ability to translocate through the cell membrane while carrying large cargo biomolecules has been the topic of pre-clinical and clinical trials. The ability to deliver cargo complexes through membranes yields potential for therapeutics and diagnostics for diseases such as cancer. Upon cellular entry, some CPPs have the ability to target specific organelles. CPP-based intracellular targeting strategies hold tremendous potential as they can improve efficacy and reduce toxicities and side effects. Further, recent clinical trials show a significant potential for future CPP-based cancer treatment. In this review, we summarize recent advances in CPPs based on systematic searches in PubMed, Embase, Web of Science, and Scopus databases until 30 September 2022. We highlight targeted delivery and explore the potential uses for CPPs as diagnostics, drug delivery, and intrinsic anti-cancer agents.
引用
收藏
页数:17
相关论文
共 166 条
[1]   High efficacy gold-KDEL peptide-siRNA nanoconstruct-mediated transfection in C2C12 myoblasts and myotubes [J].
Acharya, Suresh ;
Hill, Rodney Allan .
NANOMEDICINE-NANOTECHNOLOGY BIOLOGY AND MEDICINE, 2014, 10 (02) :329-337
[2]   CPPsite 2.0: a repository of experimentally validated cell-penetrating peptides [J].
Agrawal, Piyush ;
Bhalla, Sherry ;
Usmani, Salman Sadullah ;
Singh, Sandeep ;
Chaudhary, Kumardeep ;
Raghava, Gajendra P. S. ;
Gautam, Ankur .
NUCLEIC ACIDS RESEARCH, 2016, 44 (D1) :D1098-D1103
[3]   pVEC hydrophobic N-terminus is critical for antibacterial activity [J].
Alaybeyoglu, Begum ;
Akbulut, Berna Sariyar ;
Ozkirimli, Elif .
JOURNAL OF PEPTIDE SCIENCE, 2018, 24 (06)
[4]   Insights into membrane translocation of the cell-penetrating peptide pVEC from molecular dynamics calculations [J].
Alaybeyoglu, Begum ;
Akbulut, Berna Sariyar ;
Ozkirimli, Elif .
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2016, 34 (11) :2387-2398
[5]   Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides [J].
Allen, Jason ;
Pellois, Jean-Philippe .
SCIENTIFIC REPORTS, 2022, 12 (01)
[6]   Generation of Endosomolytic Reagents by Branching of Cell-Penetrating Peptides: Tools for the Delivery of Bioactive Compounds to Live Cells in Cis or Trans [J].
Angeles-Boza, Alfredo M. ;
Erazo-Oliveras, Alfredo ;
Lee, Ya-Jung ;
Pellois, Jean-Philippe .
BIOCONJUGATE CHEMISTRY, 2010, 21 (12) :2164-2167
[7]   Intelligent biosynthetic nanobiomaterials for hyperthermic combination chemotherapy and thermal drug targeting of HSP90 inhibitor geldanamycin [J].
Bae, Younsoo ;
Buresh, Rita A. ;
Williamson, Tracy P. ;
Chen, Tze-Haw Howard ;
Furgeson, Darin Y. .
JOURNAL OF CONTROLLED RELEASE, 2007, 122 (01) :16-23
[8]   Mitochondria-targeting drug conjugates for cytotoxic, anti-oxidizing and sensing purposes: current strategies and future perspectives [J].
Battogtokh, Gantumur ;
Choi, Yeon Su ;
Kang, Dong Seop ;
Park, Sang Jun ;
Shim, Min Suk ;
Huh, Kang Moo ;
Cho, Yong-Yeon ;
Lee, Joo Young ;
Lee, Hye Suk ;
Kang, Han Chang .
ACTA PHARMACEUTICA SINICA B, 2018, 8 (06) :862-880
[9]   Structural Elucidation of the Cell-Penetrating Penetratin Peptide in Model Membranes at the Atomic Level: Probing Hydrophobic Interactions in the Blood-Brain Barrier [J].
Bera, Swapna ;
Kar, Rajiv K. ;
Mondal, Susanta ;
Pahan, Kalipada ;
Bhunia, Anirban .
BIOCHEMISTRY, 2016, 55 (35) :4982-4996
[10]   Time-Resolved Fluorescence and Essential Dynamics Study on the Structural Heterogeneity of p53DBD Bound to the Anticancer p28 Peptide [J].
Bizzarri, Anna Rita ;
Cannistraro, Salvatore .
JOURNAL OF PHYSICAL CHEMISTRY B, 2020, 124 (44) :9820-9828