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Article ; Online: Enhanced Secretion of Functional Insulin with DNA-Functionalized Gold Nanoparticles in Cells.

Chan, Kian Ping / Chao, Sheng-Hao / Kah, James Chen Yong

ACS biomaterials science & engineering

2019 Volume 5, Issue 3, Page(s) 1602–1610

Abstract: We have previously shown the use of gold nanoparticles (AuNPs) functionalized with DNA (AuNP-DNA) to increase insulin mRNA translation in a cell-free system. In this study, we translate the concept into a whole cell system to demonstrate functionality ... ...

Abstract	We have previously shown the use of gold nanoparticles (AuNPs) functionalized with DNA (AuNP-DNA) to increase insulin mRNA translation in a cell-free system. In this study, we translate the concept into a whole cell system to demonstrate functionality despite the additional complexity of intracellular delivery and mRNA translation inside living cells. We selected an insulin-secreting pancreatic islet cell line, RIN-5F, as our model and designed a DNA oligomer (insDNA) that is complementary to the 3'-untranslated region of insulin mRNA for conjugation to AuNPs (AuNP-insDNA). AuNP-insDNA was stable in the extracellular environment of RIN-5F cells for up to 24 h, without eliciting any cell toxicity. Upon cellular entry, AuNP-insDNA was able to sustain enhanced insulin secretion from 6 to 12 h post-incubation, peaking at 10 h with an enhancement factor of 1.69-fold. This enhancement was not observed when insDNA was removed or replaced with poly thymine or poly adenine DNAs. The enhanced insulin secreted was 100% functional and capable of binding to its insulin receptor. The outcome of this study demonstrated the feasibility of AuNP-DNA to enhance the synthesis of proteins in whole cells and could serve as a new direction of invoking a patient's own beta cells to increase insulin secretion for treatment of diabetes.
Language	English
Publishing date	2019-02-19
Publishing country	United States
Document type	Journal Article
ISSN	2373-9878
ISSN (online)	2373-9878
DOI	10.1021/acsbiomaterials.9b00032
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Article ; Online: Exploiting Protein Corona around Gold Nanoparticles Conjugated to p53 Activating Peptides To Increase the Level of Stable p53 Proteins in Cells.

Chan, Kian Ping / Chao, Sheng-Hao / Kah, James Chen Yong

Bioconjugate chemistry

2019 Volume 30, Issue 3, Page(s) 920–930

Abstract: Therapeutic peptides suffer from major drawbacks such as peptide degradation in vivo due to proteolysis. Gold nanoparticles (AuNPs) are an effective carrier for therapeutic peptides that improve their stability in vivo, while also enabling nonspecific ... ...

Abstract	Therapeutic peptides suffer from major drawbacks such as peptide degradation in vivo due to proteolysis. Gold nanoparticles (AuNPs) are an effective carrier for therapeutic peptides that improve their stability in vivo, while also enabling nonspecific adsorption of complementary proteins to enhance their effectiveness. Using p53 peptide as a model known to disrupt the intracellular MDM2-p53 protein-protein interaction which tags the endogenous p53 proteins for degradation, we conjugated p53 peptides to AuNPs (AuNP-p53) and examined the functionality of AuNP-p53 to release the endogenous p53 proteins from being tagged for degradation, thereby increasing the level of stable p53 proteins in acute myeloid leukemia 2 (AML2) cells. We found that AuNPs did not just protect conjugated p53 peptides from trypsin degradation, but also helped to recruit 56.5% and 26.4% of total MDM2 and p53 proteins in the cells to form a protein corona around AuNP-p53. The proximity of MDM2/p53 complexes and p53 peptide on the surface of AuNP-p53 facilitated the action of p53 peptides to cause a sustained elevation of the p53 level in AML2 cells up to 6 h, which was not possible with free p53 peptide alone at the same concentration. Even a 20-fold higher concentration of free p53 peptide caused only a short-lived elevated p53 level of 1 h. The outcome of this study highlights the utility of combining conjugated ligands and complementary protein adsorption on nanoparticles to improve the biological functionality of the therapeutic ligands.
MeSH term(s)	Cell Line, Tumor ; Gold/chemistry ; Humans ; Metal Nanoparticles/chemistry ; Peptides/chemistry ; Protein Corona/chemistry ; Proto-Oncogene Proteins c-mdm2/chemistry ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Peptides ; Protein Corona ; TP53 protein, human ; Tumor Suppressor Protein p53 ; Gold (7440-57-5) ; MDM2 protein, human (EC 2.3.2.27) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
Language	English
Publishing date	2019-02-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1024041-x
ISSN	1520-4812 ; 1043-1802
ISSN (online)	1520-4812
ISSN	1043-1802
DOI	10.1021/acs.bioconjchem.9b00032
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Article ; Online: Universal mRNA Translation Enhancement with Gold Nanoparticles Conjugated to Oligonucleotides with a Poly(T) Sequence.

Chan, Kian Ping / Chao, Sheng-Hao / Kah, James Chen Yong

ACS applied materials & interfaces

2018 Volume 10, Issue 6, Page(s) 5203–5212

Abstract: DNA-conjugated gold nanoparticles (AuNPs) have been shown to enhance the translation of mRNA. However, the specific sequence on the DNA dictates the specific mRNA to be enhanced. This study describes poly(thymine)-functionalized AuNPs (AuNP-p(T)DNA) ... ...

Abstract	DNA-conjugated gold nanoparticles (AuNPs) have been shown to enhance the translation of mRNA. However, the specific sequence on the DNA dictates the specific mRNA to be enhanced. This study describes poly(thymine)-functionalized AuNPs (AuNP-p(T)DNA) capable of enhancing the translation of any mRNA template that is incorporated into pcDNA6 vector with bovine growth hormone (BGH) polyadenylation signal (P(A)). We demonstrated this by incorporating four genes: green fluorescence protein (GFP), general control nonderepressible 5 (GCN5), cAMP-responsive element binding protein 1 (CREB1), and X-box-binding protein 1-spliced (XBP-1S) separately into pcDNA6 vector with BGH P(A) before their expression in HeLa lysate. The addition of AuNP-p(T)DNA to HeLa lysate containing GFP, GCN5, CREB1, and XBP-1S mRNA increased protein synthesis 1.80, 1.99, 1.95, and 2.20 times, respectively. Similar translation enhancement was also observed in a multiplex reaction containing the mRNA of three genes together in the lysate. Complementary p(T)DNA hybridization to the poly(A) tail of the mRNA was critical as the removal of either p(T)DNA or BGH P(A) in XBP-1S mRNA or the replacement of p(T)DNA with p(A)DNA reduced the translation back to baseline level. Finally, an optimum length of 25 nucleotides for the DNA oligomer and a AuNP-p(T)DNA:mRNA ratio of 0.658 achieved a 3.08-fold translation enhancement. The AuNP-p(T)DNA nanoconstruct could be incorporated into commercial cell-free protein synthesis kits as a universal translation enhancer.
MeSH term(s)	Animals ; Cattle ; DNA ; Gold ; Metal Nanoparticles ; Oligonucleotides ; RNA, Messenger
Chemical Substances	Oligonucleotides ; RNA, Messenger ; Gold (7440-57-5) ; DNA (9007-49-2)
Language	English
Publishing date	2018-02-02
Publishing country	United States
Document type	Journal Article
ISSN	1944-8252
ISSN (online)	1944-8252
DOI	10.1021/acsami.7b16390
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Article: HEXIM1 Peptide Exhibits Antimicrobial Activity Against Antibiotic Resistant Bacteria Through Guidance of Cell Penetrating Peptide.

Ho, Pooi Leng / Ong, Han Kee / Teo, Jeanette / Ow, Dave Siak-Wei / Chao, Sheng-Hao

Frontiers in microbiology

2019 Volume 10, Page(s) 203

Abstract: The emergence of antibiotic resistant bacteria is one of the biggest threats to human health worldwide. In 2017, World Health Organization listed the world's most dangerous antibiotic-resistant bacteria or "superbugs," such as carbapenem- ... ...

Abstract	The emergence of antibiotic resistant bacteria is one of the biggest threats to human health worldwide. In 2017, World Health Organization listed the world's most dangerous antibiotic-resistant bacteria or "superbugs," such as carbapenem-resistant
Language	English
Publishing date	2019-02-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2019.00203
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Article ; Online: Tumor Suppressor p14ARF Enhances IFN-γ-Activated Immune Response by Inhibiting PIAS1 via SUMOylation.

Alagu, Jennifer / Itahana, Yoko / Sim, Faizal / Chao, Sheng-Hao / Bi, Xuezhi / Itahana, Koji

Journal of immunology (Baltimore, Md. : 1950)

2018 Volume 201, Issue 2, Page(s) 451–464

Abstract: The ability of cells to induce the appropriate transcriptional response to inflammatory stimuli is crucial for the timely induction of host defense mechanisms. Although a role for tumor suppressor p14ARF (ARF) in the innate immune response was previously ...

Abstract	The ability of cells to induce the appropriate transcriptional response to inflammatory stimuli is crucial for the timely induction of host defense mechanisms. Although a role for tumor suppressor p14ARF (ARF) in the innate immune response was previously demonstrated, the underlying mechanism is still unclear. ARF is a potent upregulator of protein SUMOylation; however, no association of this function with the immune system has been made. In this study, we show the unique role of ARF in IFN-γ-induced immune response using human cell lines. Through a systematic search of proteins SUMOylated by ARF, we identified PIAS1, an inhibitor of IFN-activated transcription factor STAT1, as a novel ARF-binding partner and SUMOylation target. In response to IFN-γ treatment, ARF promoted PIAS1 SUMOylation to inhibit the ability of PIAS1 to attenuate IFN-γ response. Wild-type, but not ARF mutants unable to enhance PIAS1 SUMOylation, prevented the PIAS1-mediated inhibition of IFN-γ response. Conversely, the SUMO-deconjugase SENP1 deSUMOylated PIAS1 to reactivate PIAS1 that was inhibited by ARF. These findings suggest that PIAS1 function is negatively modulated by SUMO modification and that SUMOylation by ARF is required to inhibit PIAS1 activity and restore IFN-γ-induced transcription. In the presence of ARF, in which case PIAS1 is inhibited, depletion of PIAS1 did not have an additive effect on IFN-γ response, suggesting that ARF-mediated enhancement of IFN-γ response is mainly due to PIAS1 inhibition. Our findings reveal a novel function of ARF to inhibit PIAS1 by enhancing SUMOylation to promote the robust induction of IFN-γ response.
MeSH term(s)	Cell Line ; Cell Line, Tumor ; HEK293 Cells ; Humans ; Immunity, Innate/immunology ; Inflammation/immunology ; Interferon-gamma/immunology ; Protein Inhibitors of Activated STAT/immunology ; STAT1 Transcription Factor/immunology ; Small Ubiquitin-Related Modifier Proteins/immunology ; Sumoylation/immunology ; Transcription, Genetic/immunology ; Tumor Suppressor Protein p14ARF/immunology ; Up-Regulation/immunology
Chemical Substances	PIAS1 protein, human ; Protein Inhibitors of Activated STAT ; STAT1 Transcription Factor ; Small Ubiquitin-Related Modifier Proteins ; Tumor Suppressor Protein p14ARF ; Interferon-gamma (82115-62-6)
Language	English
Publishing date	2018-05-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1800327
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Article ; Online: XBP-1, a Cellular Target for the Development of Novel Anti-viral Strategies.

Ong, Han Kee / Soo, Benjamin P C / Chu, Kai Ling / Chao, Sheng-Hao

Current protein & peptide science

2017 Volume 19, Issue 2, Page(s) 145–154

Abstract: X-box binding protein 1 (XBP-1) is a key regulator of the unfolded protein response (UPR), which is activated in response to endoplasmic reticulum (ER) stress. Cells contain two protein isoforms of XBP-1, the active isoform (XBP-1S) and the inactive ... ...

Abstract	X-box binding protein 1 (XBP-1) is a key regulator of the unfolded protein response (UPR), which is activated in response to endoplasmic reticulum (ER) stress. Cells contain two protein isoforms of XBP-1, the active isoform (XBP-1S) and the inactive isoform (XBP-1U). Induction of UPR leads to the generation of XBP-1S while XBP-1U is dominant in ER stress-free cells. XBP-1S is a transcriptional activator and regulates the expression of a subset of UPR genes. Importantly, recent studies have demonstrated the essential role of XBP-1S in various human diseases, such as viral infections. Many viruses have evolved to manipulate UPR/XBP-1 of the infected cells to promote viral survival and replication. In this review, we will summarize the current findings on the involvement of XBP-1 in viral infection/ replication and discuss the potential anti-viral strategies by targeting XBP-1.
MeSH term(s)	Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Endoplasmic Reticulum Stress ; Humans ; Protein Folding ; Transcription Factors/metabolism ; Unfolded Protein Response ; Virus Diseases/drug therapy ; Virus Diseases/metabolism ; Virus Diseases/virology ; Virus Replication ; X-Box Binding Protein 1/metabolism
Chemical Substances	Antiviral Agents ; Transcription Factors ; X-Box Binding Protein 1
Language	English
Publishing date	2017-09-13
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2045662-1
ISSN	1875-5550 ; 1389-2037
ISSN (online)	1875-5550
ISSN	1389-2037
DOI	10.2174/1389203718666170911144812
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Article: Identification of lysine K18 acetylation on histone H3 peptide using gold nanoparticles’ aggregation behaviour

Li, Ning / Chao, Sheng-Hao / Lew, Qiao Jing / Su, Xiaodi / Sutarlie, Laura

Amino acids. 2016 Apr., v. 48, no. 4

2016

Abstract: Acetylation of histones, the major protein component of eukaryotic chromosomes, contributes to the epigenetic regulation of gene expression and is also involved in cancer development. A recent study revealed the correlation between tumour formation and ... ...

Abstract	Acetylation of histones, the major protein component of eukaryotic chromosomes, contributes to the epigenetic regulation of gene expression and is also involved in cancer development. A recent study revealed the correlation between tumour formation and acetylation level of lysine K18 on histone H3. In this study, we developed two colorimetric in vitro assays using gold nanoparticles (AuNPs) for identification of lysine K18 acetylation on histone H3 peptide. In assay I, citrate ion-capped AuNP without further modification was employed. Simply mixing the K18 peptide with AuNP solution leads to distinct particle aggregation, relative to that by non-acetylated or lysine K14 acetylated control peptides. In assay II, an AuNP–peptide–antibody composite was synthesized and used as both the sensing probe and the transducing element. By mixing the sample peptides with the composite solution followed by PBS screening, different aggregation behaviours were observed between the K18 acetylated target peptide and the control sequences. Both assays are capable of identifying the acetylated peptides, and also differentiating the distinctive acetylation positions that differ merely by a distance of three amino acids.
Keywords	acetylation ; aggregation behavior ; chromosomes ; citrates ; colorimetry ; epigenetics ; gene expression regulation ; histones ; in vitro studies ; lysine ; mixing ; nanogold ; neoplasms ; peptides ; screening
Language	English
Dates of publication	2016-04
Size	p. 1023-1031.
Publishing place	Springer Vienna
Document type	Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-015-2148-1
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Brd4 and HEXIM1: multiple roles in P-TEFb regulation and cancer.

Chen, Ruichuan / Yik, Jasper H N / Lew, Qiao Jing / Chao, Sheng-Hao

BioMed research international

2014 Volume 2014, Page(s) 232870

Abstract: Bromodomain-containing protein 4 (Brd4) and hexamethylene bisacetamide (HMBA) inducible protein 1 (HEXIM1) are two opposing regulators of the positive transcription elongation factor b (P-TEFb), which is the master modulator of RNA polymerase II during ... ...

Abstract	Bromodomain-containing protein 4 (Brd4) and hexamethylene bisacetamide (HMBA) inducible protein 1 (HEXIM1) are two opposing regulators of the positive transcription elongation factor b (P-TEFb), which is the master modulator of RNA polymerase II during transcriptional elongation. While Brd4 recruits P-TEFb to promoter-proximal chromatins to activate transcription, HEXIM1 sequesters P-TEFb into an inactive complex containing the 7SK small nuclear RNA. Besides regulating P-TEFb's transcriptional activity, recent evidence demonstrates that both Brd4 and HEXIM1 also play novel roles in cell cycle progression and tumorigenesis. Here we will discuss the current knowledge on Brd4 and HEXIM1 and their implication as novel therapeutic options against cancer.
MeSH term(s)	Amino Acid Sequence ; Humans ; Models, Biological ; Molecular Sequence Data ; Neoplasms/metabolism ; Positive Transcriptional Elongation Factor B/metabolism ; RNA-Binding Proteins/metabolism ; Transcription Factors/chemistry ; Transcription Factors/metabolism
Chemical Substances	RNA-Binding Proteins ; Transcription Factors ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-)
Language	English
Publishing date	2014-01-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2698540-8
ISSN	2314-6141 ; 2314-6133
ISSN (online)	2314-6141
ISSN	2314-6133
DOI	10.1155/2014/232870
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Article ; Online: Use of a novel cytotoxic HEXIM1 peptide in the directed breast cancer therapy.

Neo, Shu Hui / Lew, Qiao Jing / Koh, Ser Mei / Zheng, Lu / Bi, Xuezhi / Chao, Sheng-Hao

Oncotarget

2016 Volume 7, Issue 5, Page(s) 5483–5494

Abstract: Hexamethylene bisacetamide-inducible protein 1 (HEXIM1) is best known as the inhibitor of positive transcription elongation factor b (P-TEFb) and is recently identified as a novel positive regulator of p53. We previously showed the basic region (BR) of ... ...

Abstract	Hexamethylene bisacetamide-inducible protein 1 (HEXIM1) is best known as the inhibitor of positive transcription elongation factor b (P-TEFb) and is recently identified as a novel positive regulator of p53. We previously showed the basic region (BR) of HEXIM1 mediates the binding of HEXIM1 to a nucleolar protein, nucleophosmin (NPM), and can be ubiquitinated by human double minute 2 protein. Here we identify a cytotoxic peptide derived from the BR of HEXIM1. When fused with a cell-penetrating peptide, the HEXIM1 BR peptide triggers rapid cytotoxic effect independent of p53. Similarly, when the BR peptide is linked with a breast cancer cell targeting peptide, LTV, the LTV-BR fusion peptide exhibits specific killing of breast cancer cells, which is not observed with the commonly used cytotoxic peptide, KLA. Importantly, the BR peptide fails to enter cells by itself and does not induce any cytotoxic effects when it is not guided by any cell-penetrating or cancer targeting peptides. We showed that HEXIM1 BR peptide depolarizes mitochondrial membrane potential in a p53-dependent manner and its cell-killing activity is not suppressed by caspase inhibition. Furthermore, we observed an accumulation of the internalized BR peptide in the nucleoli of treated cells and an altered localization of NPM. These results illustrate a novel mechanism which the BR peptide induces cell death and can potentially be used as a novel therapeutic strategy against breast cancer.
MeSH term(s)	Apoptosis ; Blotting, Western ; Breast Neoplasms/drug therapy ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Proliferation ; Female ; Fluorescent Antibody Technique ; Humans ; Peptide Fragments/pharmacology ; RNA-Binding Proteins/antagonists & inhibitors ; RNA-Binding Proteins/metabolism ; Transcription Factors ; Transcription, Genetic ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	HEXIM1 protein, human ; Peptide Fragments ; RNA-Binding Proteins ; TP53 protein, human ; Transcription Factors ; Tumor Suppressor Protein p53
Language	English
Publishing date	2016-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.6794
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Article ; Online: Identification of lysine K18 acetylation on histone H3 peptide using gold nanoparticles' aggregation behaviour.

Li, Ning / Sutarlie, Laura / Lew, Qiao Jing / Chao, Sheng-Hao / Su, Xiaodi

Amino acids

2015 Volume 48, Issue 4, Page(s) 1023–1031

Abstract	Acetylation of histones, the major protein component of eukaryotic chromosomes, contributes to the epigenetic regulation of gene expression and is also involved in cancer development. A recent study revealed the correlation between tumour formation and acetylation level of lysine K18 on histone H3. In this study, we developed two colorimetric in vitro assays using gold nanoparticles (AuNPs) for identification of lysine K18 acetylation on histone H3 peptide. In assay I, citrate ion-capped AuNP without further modification was employed. Simply mixing the K18 peptide with AuNP solution leads to distinct particle aggregation, relative to that by non-acetylated or lysine K14 acetylated control peptides. In assay II, an AuNP-peptide-antibody composite was synthesized and used as both the sensing probe and the transducing element. By mixing the sample peptides with the composite solution followed by PBS screening, different aggregation behaviours were observed between the K18 acetylated target peptide and the control sequences. Both assays are capable of identifying the acetylated peptides, and also differentiating the distinctive acetylation positions that differ merely by a distance of three amino acids.
MeSH term(s)	Acetylation ; Amino Acid Sequence ; Antibodies/chemistry ; Biosensing Techniques ; Chromatin/chemistry ; Chromatin/metabolism ; Colorimetry/methods ; Colorimetry/standards ; Flocculation ; Gold/chemistry ; Histones/chemistry ; Histones/metabolism ; Lysine/chemistry ; Lysine/metabolism ; Metal Nanoparticles/chemistry ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/metabolism ; Protein Processing, Post-Translational
Chemical Substances	Antibodies ; Chromatin ; Histones ; Peptides ; Gold (7440-57-5) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2015-12-30
Publishing country	Austria
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-015-2148-1
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