Anticancer effect of rationally designed α-helical amphiphilic peptides
Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Pan, Fang [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022transfer abstract |
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| Übergeordnetes Werk: |
Enthalten in: Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills - Han, Zhe ELSEVIER, 2019, an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:220 ; year:2022 ; pages:0 |
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| DOI / URN: |
10.1016/j.colsurfb.2022.112841 |
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| 245 | 1 | 0 | |a Anticancer effect of rationally designed α-helical amphiphilic peptides |
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| 520 | |a Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. | ||
| 520 | |a Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. | ||
| 650 | 7 | |a Membrane-lytic peptides |2 Elsevier | |
| 650 | 7 | |a Membrane disruption |2 Elsevier | |
| 650 | 7 | |a Anticancer activity |2 Elsevier | |
| 650 | 7 | |a Amphiphilic peptides |2 Elsevier | |
| 650 | 7 | |a Anticancer peptides |2 Elsevier | |
| 700 | 1 | |a Li, Yueping |4 oth | |
| 700 | 1 | |a Ding, Yujie |4 oth | |
| 700 | 1 | |a Lv, Songwei |4 oth | |
| 700 | 1 | |a You, Rongrong |4 oth | |
| 700 | 1 | |a Hadianamrei, Roja |4 oth | |
| 700 | 1 | |a Tomeh, Mhd Anas |4 oth | |
| 700 | 1 | |a Zhao, Xiubo |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Han, Zhe ELSEVIER |t Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills |d 2019 |d an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin |g Amsterdam [u.a.] |w (DE-627)ELV003763382 |
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10.1016/j.colsurfb.2022.112841 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001978.pica (DE-627)ELV059640227 (ELSEVIER)S0927-7765(22)00524-0 DE-627 ger DE-627 rakwb eng 540 VZ Pan, Fang verfasserin aut Anticancer effect of rationally designed α-helical amphiphilic peptides 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Membrane-lytic peptides Elsevier Membrane disruption Elsevier Anticancer activity Elsevier Amphiphilic peptides Elsevier Anticancer peptides Elsevier Li, Yueping oth Ding, Yujie oth Lv, Songwei oth You, Rongrong oth Hadianamrei, Roja oth Tomeh, Mhd Anas oth Zhao, Xiubo oth Enthalten in Elsevier Science Han, Zhe ELSEVIER Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills 2019 an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin Amsterdam [u.a.] (DE-627)ELV003763382 volume:220 year:2022 pages:0 https://doi.org/10.1016/j.colsurfb.2022.112841 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 220 2022 0 |
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10.1016/j.colsurfb.2022.112841 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001978.pica (DE-627)ELV059640227 (ELSEVIER)S0927-7765(22)00524-0 DE-627 ger DE-627 rakwb eng 540 VZ Pan, Fang verfasserin aut Anticancer effect of rationally designed α-helical amphiphilic peptides 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Membrane-lytic peptides Elsevier Membrane disruption Elsevier Anticancer activity Elsevier Amphiphilic peptides Elsevier Anticancer peptides Elsevier Li, Yueping oth Ding, Yujie oth Lv, Songwei oth You, Rongrong oth Hadianamrei, Roja oth Tomeh, Mhd Anas oth Zhao, Xiubo oth Enthalten in Elsevier Science Han, Zhe ELSEVIER Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills 2019 an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin Amsterdam [u.a.] (DE-627)ELV003763382 volume:220 year:2022 pages:0 https://doi.org/10.1016/j.colsurfb.2022.112841 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 220 2022 0 |
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10.1016/j.colsurfb.2022.112841 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001978.pica (DE-627)ELV059640227 (ELSEVIER)S0927-7765(22)00524-0 DE-627 ger DE-627 rakwb eng 540 VZ Pan, Fang verfasserin aut Anticancer effect of rationally designed α-helical amphiphilic peptides 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Membrane-lytic peptides Elsevier Membrane disruption Elsevier Anticancer activity Elsevier Amphiphilic peptides Elsevier Anticancer peptides Elsevier Li, Yueping oth Ding, Yujie oth Lv, Songwei oth You, Rongrong oth Hadianamrei, Roja oth Tomeh, Mhd Anas oth Zhao, Xiubo oth Enthalten in Elsevier Science Han, Zhe ELSEVIER Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills 2019 an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin Amsterdam [u.a.] (DE-627)ELV003763382 volume:220 year:2022 pages:0 https://doi.org/10.1016/j.colsurfb.2022.112841 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 220 2022 0 |
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10.1016/j.colsurfb.2022.112841 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001978.pica (DE-627)ELV059640227 (ELSEVIER)S0927-7765(22)00524-0 DE-627 ger DE-627 rakwb eng 540 VZ Pan, Fang verfasserin aut Anticancer effect of rationally designed α-helical amphiphilic peptides 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Membrane-lytic peptides Elsevier Membrane disruption Elsevier Anticancer activity Elsevier Amphiphilic peptides Elsevier Anticancer peptides Elsevier Li, Yueping oth Ding, Yujie oth Lv, Songwei oth You, Rongrong oth Hadianamrei, Roja oth Tomeh, Mhd Anas oth Zhao, Xiubo oth Enthalten in Elsevier Science Han, Zhe ELSEVIER Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills 2019 an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin Amsterdam [u.a.] (DE-627)ELV003763382 volume:220 year:2022 pages:0 https://doi.org/10.1016/j.colsurfb.2022.112841 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 220 2022 0 |
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10.1016/j.colsurfb.2022.112841 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001978.pica (DE-627)ELV059640227 (ELSEVIER)S0927-7765(22)00524-0 DE-627 ger DE-627 rakwb eng 540 VZ Pan, Fang verfasserin aut Anticancer effect of rationally designed α-helical amphiphilic peptides 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. Membrane-lytic peptides Elsevier Membrane disruption Elsevier Anticancer activity Elsevier Amphiphilic peptides Elsevier Anticancer peptides Elsevier Li, Yueping oth Ding, Yujie oth Lv, Songwei oth You, Rongrong oth Hadianamrei, Roja oth Tomeh, Mhd Anas oth Zhao, Xiubo oth Enthalten in Elsevier Science Han, Zhe ELSEVIER Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills 2019 an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin Amsterdam [u.a.] (DE-627)ELV003763382 volume:220 year:2022 pages:0 https://doi.org/10.1016/j.colsurfb.2022.112841 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA AR 220 2022 0 |
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Enthalten in Pharmacy students' perceptions toward peer assessment and its use in teaching patient presentation skills Amsterdam [u.a.] volume:220 year:2022 pages:0 |
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Pan, Fang @@aut@@ Li, Yueping @@oth@@ Ding, Yujie @@oth@@ Lv, Songwei @@oth@@ You, Rongrong @@oth@@ Hadianamrei, Roja @@oth@@ Tomeh, Mhd Anas @@oth@@ Zhao, Xiubo @@oth@@ |
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Anticancer effect of rationally designed α-helical amphiphilic peptides |
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Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. |
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Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. |
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Anticancer peptides (ACPs) have attracted increasing attention in cancer therapy due to their unique mechanism of action on cancer cells. The main challenge is to establish the correlation between their physicochemical properties and their selectivity and anticancer effect, leading to a clear design strategy. In this study, a series of new α-helical short peptides (coded At1-At12) with different anticancer activities were systematically designed with different amphiphilicity based on a natural α-helical antimicrobial peptide (AMP) derived from ant. Three of the designed peptides, At7, At10 and At11, showed considerable anticancer activity with low toxicity to normal skin fibroblasts. The high selectivity of the peptides is attributed to their balanced amphiphilicity and cationic nature which favours binding to the outer membrane of negatively charged cancer cells over the neutral membrane of normal mammalian cells. In addition to rapid membrane penetration, the designed peptides also damaged the mitochondria and induced mitochondrial membrane depolarization. Moreover, these peptides were found to induce apoptosis in cancer cells by up-regulating the expression of apoptotic proteins Bax and Caspase-3, down-regulating the apoptotic protein Bcl-2, and activating the Caspase enzyme-linked reaction. The results of this study reveal the potential of these peptides for clinical applications, and provide a guidance for further development of highly selective anticancer medications. |
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