Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides
Cell-penetrating peptides (CPPs) have been discovered to deliver chemical drugs, nucleic acids, and macromolecules to permeate cell membranes, creating a novel route for exogenous substances to enter cells. Up until now, various sequence structures and fundamental action mechanisms of CPPs have been...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-08-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/16/9038 |
| _version_ | 1797432127191515136 |
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| author | Minglu Hao Lei Zhang Pu Chen |
| author_facet | Minglu Hao Lei Zhang Pu Chen |
| author_sort | Minglu Hao |
| collection | DOAJ |
| description | Cell-penetrating peptides (CPPs) have been discovered to deliver chemical drugs, nucleic acids, and macromolecules to permeate cell membranes, creating a novel route for exogenous substances to enter cells. Up until now, various sequence structures and fundamental action mechanisms of CPPs have been established. Among them, arginine-rich peptides with unique cell penetration properties have attracted substantial scientific attention. Due to the positively charged essential amino acids of the arginine-rich peptides, they can interact with negatively charged drug molecules and cell membranes through non-covalent interaction, including electrostatic interactions. Significantly, the sequence design and the penetrating mechanisms are critical. In this brief synopsis, we summarize the transmembrane processes and mechanisms of arginine-rich peptides; and outline the relationship between the function of arginine-rich peptides and the number of arginine residues, arginine optical isomers, primary sequence, secondary and ternary structures, etc. Taking advantage of the penetration ability, biomedical applications of arginine-rich peptides have been refreshed, including drug/RNA delivery systems, biosensors, and blood-brain barrier (BBB) penetration. Understanding the membrane internalization mechanisms and design strategies of CPPs will expand their potential applications in clinical trials. |
| first_indexed | 2024-03-09T09:56:46Z |
| format | Article |
| id | doaj.art-e0dc4118d71a4e768f072ba2fb79e40e |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T09:56:46Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-e0dc4118d71a4e768f072ba2fb79e40e2023-12-01T23:47:12ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-08-012316903810.3390/ijms23169038Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating PeptidesMinglu Hao0Lei Zhang1Pu Chen2Advanced Materials Institute, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250014, ChinaDepartment of Chemical Engineering, Waterloo Institute for Nanotechnology, University of Waterloo, 200 University Avenue West, Waterloo, ON N2L3G1, CanadaAdvanced Materials Institute, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250014, ChinaCell-penetrating peptides (CPPs) have been discovered to deliver chemical drugs, nucleic acids, and macromolecules to permeate cell membranes, creating a novel route for exogenous substances to enter cells. Up until now, various sequence structures and fundamental action mechanisms of CPPs have been established. Among them, arginine-rich peptides with unique cell penetration properties have attracted substantial scientific attention. Due to the positively charged essential amino acids of the arginine-rich peptides, they can interact with negatively charged drug molecules and cell membranes through non-covalent interaction, including electrostatic interactions. Significantly, the sequence design and the penetrating mechanisms are critical. In this brief synopsis, we summarize the transmembrane processes and mechanisms of arginine-rich peptides; and outline the relationship between the function of arginine-rich peptides and the number of arginine residues, arginine optical isomers, primary sequence, secondary and ternary structures, etc. Taking advantage of the penetration ability, biomedical applications of arginine-rich peptides have been refreshed, including drug/RNA delivery systems, biosensors, and blood-brain barrier (BBB) penetration. Understanding the membrane internalization mechanisms and design strategies of CPPs will expand their potential applications in clinical trials.https://www.mdpi.com/1422-0067/23/16/9038CPPsarginine-rich peptidenon-covalent interactionmechanism of internalizationpeptide designbiomedical applications |
| spellingShingle | Minglu Hao Lei Zhang Pu Chen Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides International Journal of Molecular Sciences CPPs arginine-rich peptide non-covalent interaction mechanism of internalization peptide design biomedical applications |
| title | Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides |
| title_full | Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides |
| title_fullStr | Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides |
| title_full_unstemmed | Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides |
| title_short | Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides |
| title_sort | membrane internalization mechanisms and design strategies of arginine rich cell penetrating peptides |
| topic | CPPs arginine-rich peptide non-covalent interaction mechanism of internalization peptide design biomedical applications |
| url | https://www.mdpi.com/1422-0067/23/16/9038 |
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