Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays

Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Pramod Shah [verfasserIn] Chien-Sheng Chen [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 23(2022), 2, p 712
Übergeordnetes Werk:	volume:23 ; year:2022 ; number:2, p 712

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.3390/ijms23020712

Katalog-ID:	DOAJ047824972

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allfields	10.3390/ijms23020712 doi (DE-627)DOAJ047824972 (DE-599)DOAJ0368b34ea3b04a4db950a06c5740e1b2 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Pramod Shah verfasserin aut Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry Chien-Sheng Chen verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 23(2022), 2, p 712 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:23 year:2022 number:2, p 712 https://doi.org/10.3390/ijms23020712 kostenfrei https://doaj.org/article/0368b34ea3b04a4db950a06c5740e1b2 kostenfrei https://www.mdpi.com/1422-0067/23/2/712 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2022 2, p 712
spelling	10.3390/ijms23020712 doi (DE-627)DOAJ047824972 (DE-599)DOAJ0368b34ea3b04a4db950a06c5740e1b2 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Pramod Shah verfasserin aut Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry Chien-Sheng Chen verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 23(2022), 2, p 712 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:23 year:2022 number:2, p 712 https://doi.org/10.3390/ijms23020712 kostenfrei https://doaj.org/article/0368b34ea3b04a4db950a06c5740e1b2 kostenfrei https://www.mdpi.com/1422-0067/23/2/712 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2022 2, p 712
allfields_unstemmed	10.3390/ijms23020712 doi (DE-627)DOAJ047824972 (DE-599)DOAJ0368b34ea3b04a4db950a06c5740e1b2 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Pramod Shah verfasserin aut Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry Chien-Sheng Chen verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 23(2022), 2, p 712 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:23 year:2022 number:2, p 712 https://doi.org/10.3390/ijms23020712 kostenfrei https://doaj.org/article/0368b34ea3b04a4db950a06c5740e1b2 kostenfrei https://www.mdpi.com/1422-0067/23/2/712 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2022 2, p 712
allfieldsGer	10.3390/ijms23020712 doi (DE-627)DOAJ047824972 (DE-599)DOAJ0368b34ea3b04a4db950a06c5740e1b2 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Pramod Shah verfasserin aut Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry Chien-Sheng Chen verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 23(2022), 2, p 712 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:23 year:2022 number:2, p 712 https://doi.org/10.3390/ijms23020712 kostenfrei https://doaj.org/article/0368b34ea3b04a4db950a06c5740e1b2 kostenfrei https://www.mdpi.com/1422-0067/23/2/712 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2022 2, p 712
allfieldsSound	10.3390/ijms23020712 doi (DE-627)DOAJ047824972 (DE-599)DOAJ0368b34ea3b04a4db950a06c5740e1b2 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Pramod Shah verfasserin aut Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry Chien-Sheng Chen verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 23(2022), 2, p 712 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:23 year:2022 number:2, p 712 https://doi.org/10.3390/ijms23020712 kostenfrei https://doaj.org/article/0368b34ea3b04a4db950a06c5740e1b2 kostenfrei https://www.mdpi.com/1422-0067/23/2/712 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2022 2, p 712
language	English
source	In International Journal of Molecular Sciences 23(2022), 2, p 712 volume:23 year:2022 number:2, p 712
sourceStr	In International Journal of Molecular Sciences 23(2022), 2, p 712 volume:23 year:2022 number:2, p 712
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification Biology (General) Chemistry
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container_title	International Journal of Molecular Sciences
authorswithroles_txt_mv	Pramod Shah @@aut@@ Chien-Sheng Chen @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
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topic_title	QH301-705.5 QD1-999 Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays penetratin cell penetrating peptide (CPP) antimicrobial peptide (AMP) antifungal activity proteome microarray target identification
topic	misc QH301-705.5 misc QD1-999 misc penetratin misc cell penetrating peptide (CPP) misc antimicrobial peptide (AMP) misc antifungal activity misc proteome microarray misc target identification misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc penetratin misc cell penetrating peptide (CPP) misc antimicrobial peptide (AMP) misc antifungal activity misc proteome microarray misc target identification misc Biology (General) misc Chemistry
topic_browse	misc QH301-705.5 misc QD1-999 misc penetratin misc cell penetrating peptide (CPP) misc antimicrobial peptide (AMP) misc antifungal activity misc proteome microarray misc target identification misc Biology (General) misc Chemistry
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title	Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays
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title_full	Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays
author_sort	Pramod Shah
journal	International Journal of Molecular Sciences
journalStr	International Journal of Molecular Sciences
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author_browse	Pramod Shah Chien-Sheng Chen
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author-letter	Pramod Shah
doi_str_mv	10.3390/ijms23020712
author2-role	verfasserin
title_sort	systematic screening of penetratin’s protein targets by yeast proteome microarrays
callnumber	QH301-705.5
title_auth	Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays
abstract	Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5.
abstractGer	Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5.
abstract_unstemmed	Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput <i<Saccharomyces cerevisiae</i< proteome microarrays to screen all the potential protein targets of penetratin. <i<Saccharomyces cerevisiae</i< proteome microarrays assays of penetratin followed by statistical analysis depicted 123 <i<Saccharomyces cerevisiae</i< proteins as the protein targets of penetratin out of ~5800 <i<Saccharomyces cerevisiae</i< proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays
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