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  1. Article ; Online: Development of a curriculum in cultural determinants of health and health disparities.

    Kelly, Megan L / Parente, Victoria / Redmond, Rebecca / Willis, Rheaya / Railey, Kenyon

    Journal of the National Medical Association

    2023  Volume 115, Issue 4, Page(s) 428–435

    Abstract: Introduction: Current sociopolitical events coupled with requirement modifications by the Liaison Committee on Medical Education have reinvigorated a need for training in cultural awareness and health disparities in undergraduate medical education. Many ...

    Abstract Introduction: Current sociopolitical events coupled with requirement modifications by the Liaison Committee on Medical Education have reinvigorated a need for training in cultural awareness and health disparities in undergraduate medical education. Many institutions, however, have not established longitudinal courses designed to address this content. Additionally, little is known about the change in learners' awareness of cultural determinants of health and health disparities after enrollment in such curricula. In 2016, the authors developed a yearlong required course entitled Cultural Determinants of Health and Health Disparities for first year medical students at a large university medical school in the United States. The course launched in the 2017 academic year.
    Methods: Two cohorts participated in twelve 2.5 to 3-hour multi-modal sessions focused on various aspects of healthcare delivery for marginalized populations and factors that contribute to health disparities. The Multicultural Assessment Questionnaire was used pre and post course to assess students' self-evaluated changes in knowledge, skills, and awareness related to cultural competency in healthcare.
    Results: Students' self-reported knowledge, skills, and awareness scores regarding cultural competence in health care increased from pre to post-course assessment. On the knowledge scale, students' mean score increased from 2.63 to 2.97 (P < .001), with 16% reporting a decreased score, 30% reporting no change, and 54% reporting growth. On the skills scale, students' mean score increased from 2.64 to 3.38 (P < .001), with 11% reporting a decreased score, 17% reporting no change, and 72% reporting growth. On the awareness scale, students' overall score increased from 3.76 to 3.97 (P < .05), with 16% reporting a decreased score, 50% reporting no change, and 34% reporting growth. There were no changes in KSA scores across cohorts pre and post course.
    Conclusion: Perceived knowledge, skills, and awareness related to the importance of cultural competence in healthcare delivery increased at the end of the academic year. This type of longitudinal course model could be broadly adopted at other institutions to enhance patient, peer, and future provider awareness regarding cultural impacts on care and health disparities among vulnerable populations.
    MeSH term(s) Humans ; United States ; Curriculum ; Cultural Competency/education ; Educational Measurement ; Students, Medical ; Health Inequities
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Case Reports
    ZDB-ID 419737-9
    ISSN 1943-4693 ; 0027-9684
    ISSN (online) 1943-4693
    ISSN 0027-9684
    DOI 10.1016/j.jnma.2023.06.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The roles of structural dynamics in the cellular functions of RNAs.

    Ganser, Laura R / Kelly, Megan L / Herschlag, Daniel / Al-Hashimi, Hashim M

    Nature reviews. Molecular cell biology

    2019  Volume 20, Issue 8, Page(s) 474–489

    Abstract: RNAs fold into 3D structures that range from simple helical elements to complex tertiary structures and quaternary ribonucleoprotein assemblies. The functions of many regulatory RNAs depend on how their 3D structure changes in response to a diverse array ...

    Abstract RNAs fold into 3D structures that range from simple helical elements to complex tertiary structures and quaternary ribonucleoprotein assemblies. The functions of many regulatory RNAs depend on how their 3D structure changes in response to a diverse array of cellular conditions. In this Review, we examine how the structural characterization of RNA as dynamic ensembles of conformations, which form with different probabilities and at different timescales, is improving our understanding of RNA function in cells. We discuss the mechanisms of gene regulation by microRNAs, riboswitches, ribozymes, post-transcriptional RNA modifications and RNA-binding proteins, and how the cellular environment and processes such as liquid-liquid phase separation may affect RNA folding and activity. The emerging RNA-ensemble-function paradigm is changing our perspective and understanding of RNA regulation, from in vitro to in vivo and from descriptive to predictive.
    MeSH term(s) Animals ; Gene Expression Regulation/physiology ; Humans ; RNA Folding/physiology ; RNA Processing, Post-Transcriptional/physiology ; RNA, Catalytic/genetics ; RNA, Catalytic/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances RNA, Catalytic ; RNA-Binding Proteins
    Language English
    Publishing date 2019-06-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/s41580-019-0136-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Demonstration that Small Molecules can Bind and Stabilize Low-abundance Short-lived RNA Excited Conformational States.

    Ganser, Laura R / Kelly, Megan L / Patwardhan, Neeraj N / Hargrove, Amanda E / Al-Hashimi, Hashim M

    Journal of molecular biology

    2019  Volume 432, Issue 4, Page(s) 1297–1304

    Abstract: Many promising RNA drug targets have functions that require the formation of RNA-protein complexes, but inhibiting RNA-protein interactions can prove difficult using small molecules. Regulatory RNAs have been shown to transiently form excited ... ...

    Abstract Many promising RNA drug targets have functions that require the formation of RNA-protein complexes, but inhibiting RNA-protein interactions can prove difficult using small molecules. Regulatory RNAs have been shown to transiently form excited conformational states (ESs) that remodel local aspects of secondary structure. In some cases, the ES conformation has been shown to be inactive and to be poorly recognized by protein binding partners. In these cases, specifically targeting and stabilizing the RNA ES using a small molecule provides a rational structure-based strategy for inhibiting RNA activity. However, this requires that a small molecule discriminates between two conformations of the same RNA to preferentially bind and stabilize the short-lived low-abundance ES relative to the long-lived more abundant ground state (GS). Here, we tested the feasibility of this approach by designing a mutant that inverts the conformational equilibrium of the HIV-1 transactivation response element (TAR) RNA, such that the native GS conformation becomes a low-abundance ES. Using this mutant and NMR chemical shift mapping experiments, we show that argininamide, a ligand mimic of TAR's cognate protein binding partner Tat, is able to restore a native-like conformation by preferentially binding and stabilizing the transient and low-populated ES. A synthetic small molecule optimized to bind the TAR GS also partially stabilized the ES, whereas an aminoglycoside molecule that binds RNAs nonspecifically did not preferentially stabilize the ES to a similar extent. These results support the feasibility of inhibiting RNA activity using small molecules that preferentially bind and stabilize the ES.
    MeSH term(s) HIV Long Terminal Repeat/genetics ; HIV-1/metabolism ; Magnetic Resonance Spectroscopy ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; RNA, Viral/chemistry ; RNA, Viral/genetics ; Viral Proteins/chemistry ; Viral Proteins/metabolism
    Chemical Substances RNA, Viral ; Viral Proteins
    Language English
    Publishing date 2019-12-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.12.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Probing RNA Conformational Equilibria within the Functional Cellular Context.

    Ganser, Laura R / Chu, Chia-Chieh / Bogerd, Hal P / Kelly, Megan L / Cullen, Bryan R / Al-Hashimi, Hashim M

    Cell reports

    2020  Volume 30, Issue 8, Page(s) 2472–2480.e4

    Abstract: Low-abundance short-lived non-native conformations referred to as excited states (ESs) are increasingly observed in vitro and implicated in the folding and biological activities of regulatory RNAs. We developed an approach for assessing the relative ... ...

    Abstract Low-abundance short-lived non-native conformations referred to as excited states (ESs) are increasingly observed in vitro and implicated in the folding and biological activities of regulatory RNAs. We developed an approach for assessing the relative abundance of RNA ESs within the functional cellular context. Nuclear magnetic resonance (NMR) spectroscopy was used to estimate the degree to which substitution mutations bias conformational equilibria toward the inactive ES in vitro. The cellular activity of the ES-stabilizing mutants was used as an indirect measure of the conformational equilibria within the functional cellular context. Compensatory mutations that restore the ground-state conformation were used to control for changes in sequence. Using this approach, we show that the ESs of two regulatory RNAs from HIV-1, the transactivation response element (TAR) and the Rev response element (RRE), likely form in cells with abundances comparable to those measured in vitro, and their targeted stabilization may provide an avenue for developing anti-HIV therapeutics.
    MeSH term(s) Cells/metabolism ; Cellular Microenvironment ; Genes, env ; HEK293 Cells ; HeLa Cells ; Humans ; Nucleic Acid Conformation ; RNA Stability
    Language English
    Publishing date 2020-02-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2020.02.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Publisher Correction: High-performance virtual screening by targeting a high-resolution RNA dynamic ensemble.

    Ganser, Laura R / Lee, Janghyun / Rangadurai, Atul / Merriman, Dawn K / Kelly, Megan L / Kansal, Aman D / Sathyamoorthy, Bharathwaj / Al-Hashimi, Hashim M

    Nature structural & molecular biology

    2020  Volume 27, Issue 6, Page(s) 604

    Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

    Abstract An amendment to this paper has been published and can be accessed via a link at the top of the paper.
    Language English
    Publishing date 2020-05-06
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-020-0434-4
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  6. Article ; Online: High-performance virtual screening by targeting a high-resolution RNA dynamic ensemble.

    Ganser, Laura R / Lee, Janghyun / Rangadurai, Atul / Merriman, Dawn K / Kelly, Megan L / Kansal, Aman D / Sathyamoorthy, Bharathwaj / Al-Hashimi, Hashim M

    Nature structural & molecular biology

    2018  Volume 25, Issue 5, Page(s) 425–434

    Abstract: Dynamic ensembles hold great promise in advancing RNA-targeted drug discovery. Here we subjected the transactivation response element (TAR) RNA from human immunodeficiency virus type-1 to experimental high-throughput screening against ~100,000 drug-like ... ...

    Abstract Dynamic ensembles hold great promise in advancing RNA-targeted drug discovery. Here we subjected the transactivation response element (TAR) RNA from human immunodeficiency virus type-1 to experimental high-throughput screening against ~100,000 drug-like small molecules. Results were augmented with 170 known TAR-binding molecules and used to generate sublibraries optimized for evaluating enrichment when virtually screening a dynamic ensemble of TAR determined by combining NMR spectroscopy data and molecular dynamics simulations. Ensemble-based virtual screening scores molecules with an area under the receiver operator characteristic curve of ~0.85-0.94 and with ~40-75% of all hits falling within the top 2% of scored molecules. The enrichment decreased significantly for ensembles generated from the same molecular dynamics simulations without input NMR data and for other control ensembles. The results demonstrate that experimentally determined RNA ensembles can significantly enrich libraries with true hits and that the degree of enrichment is dependent on the accuracy of the ensemble.
    MeSH term(s) Drug Discovery/methods ; HIV Long Terminal Repeat/genetics ; HIV-1/genetics ; High-Throughput Screening Assays ; Humans ; Magnetic Resonance Spectroscopy ; Molecular Dynamics Simulation ; RNA, Viral/genetics ; Small Molecule Libraries/pharmacology
    Chemical Substances RNA, Viral ; Small Molecule Libraries
    Language English
    Publishing date 2018-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-018-0062-4
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  7. Article ; Online: Understanding the characteristics of nonspecific binding of drug-like compounds to canonical stem-loop RNAs and their implications for functional cellular assays.

    Kelly, Megan L / Chu, Chia-Chieh / Shi, Honglue / Ganser, Laura R / Bogerd, Hal P / Huynh, Kelly / Hou, Yuze / Cullen, Bryan R / Al-Hashimi, Hashim M

    RNA (New York, N.Y.)

    2020  Volume 27, Issue 1, Page(s) 12–26

    Abstract: Identifying small molecules that selectively bind an RNA target while discriminating against all other cellular RNAs is an important challenge in RNA-targeted drug discovery. Much effort has been directed toward identifying drug-like small molecules that ...

    Abstract Identifying small molecules that selectively bind an RNA target while discriminating against all other cellular RNAs is an important challenge in RNA-targeted drug discovery. Much effort has been directed toward identifying drug-like small molecules that minimize electrostatic and stacking interactions that lead to nonspecific binding of aminoglycosides and intercalators to many stem-loop RNAs. Many such compounds have been reported to bind RNAs and inhibit their cellular activities. However, target engagement and cellular selectivity assays are not routinely performed, and it is often unclear whether functional activity directly results from specific binding to the target RNA. Here, we examined the propensities of three drug-like compounds, previously shown to bind and inhibit the cellular activities of distinct stem-loop RNAs, to bind and inhibit the cellular activities of two unrelated HIV-1 stem-loop RNAs: the transactivation response element (TAR) and the rev response element stem IIB (RREIIB). All compounds bound TAR and RREIIB in vitro, and two inhibited TAR-dependent transactivation and RRE-dependent viral export in cell-based assays while also exhibiting off-target interactions consistent with nonspecific activity. A survey of X-ray and NMR structures of RNA-small molecule complexes revealed that aminoglycosides and drug-like molecules form hydrogen bonds with functional groups commonly accessible in canonical stem-loop RNA motifs, in contrast to ligands that specifically bind riboswitches. Our results demonstrate that drug-like molecules can nonspecifically bind stem-loop RNAs most likely through hydrogen bonding and electrostatic interactions and reinforce the importance of assaying for off-target interactions and RNA selectivity in vitro and in cells when assessing novel RNA-binders.
    MeSH term(s) Aminoglycosides/chemistry ; Aminoglycosides/metabolism ; Aminoglycosides/pharmacology ; Base Pairing ; Base Sequence ; Binding Sites ; Biological Assay ; Drug Discovery ; Genes, env/drug effects ; HIV Long Terminal Repeat/drug effects ; HIV-1/drug effects ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Hydrogen Bonding ; Isoquinolines/chemistry ; Isoquinolines/metabolism ; Isoquinolines/pharmacology ; Nucleic Acid Conformation ; Pentamidine/chemistry ; Pentamidine/metabolism ; Pentamidine/pharmacology ; RNA, Viral/antagonists & inhibitors ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/metabolism ; Small Molecule Libraries/pharmacology ; Static Electricity ; Transcriptional Activation/drug effects ; Yohimbine/chemistry ; Yohimbine/metabolism ; Yohimbine/pharmacology
    Chemical Substances Aminoglycosides ; Isoquinolines ; RNA, Viral ; Small Molecule Libraries ; Yohimbine (2Y49VWD90Q) ; Pentamidine (673LC5J4LQ)
    Language English
    Publishing date 2020-10-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.076257.120
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  8. Article ; Online: Disruption of a ∼23-24 nucleotide small RNA pathway elevates DNA damage responses in

    Lee, Suzanne R / Pollard, Daniel A / Galati, Domenico F / Kelly, Megan L / Miller, Brian / Mong, Christina / Morris, Megan N / Roberts-Nygren, Kerry / Kapler, Geoffrey M / Zinkgraf, Matthew / Dang, Hung Q / Branham, Erica / Sasser, Jason / Tessier, Erin / Yoshiyama, Courtney / Matsumoto, Maya / Turman, Gaea

    Molecular biology of the cell

    2021  Volume 32, Issue 15, Page(s) 1335–1346

    Abstract: Endogenous RNA interference (RNAi) pathways regulate a wide range of cellular processes in diverse eukaryotes, yet in the ciliated eukaryote, ...

    Abstract Endogenous RNA interference (RNAi) pathways regulate a wide range of cellular processes in diverse eukaryotes, yet in the ciliated eukaryote,
    MeSH term(s) DNA/metabolism ; DNA Breaks, Double-Stranded ; DNA Repair ; Evolution, Molecular ; Gene Expression Profiling ; Gene Expression Regulation ; Protozoan Proteins ; RNA, Small Interfering/metabolism ; Rad51 Recombinase/genetics ; Recombinational DNA Repair ; Sequence Analysis, RNA ; Tetrahymena thermophila/genetics ; Tetrahymena thermophila/metabolism
    Chemical Substances Protozoan Proteins ; RNA, Small Interfering ; DNA (9007-49-2) ; Rad51 Recombinase (EC 2.7.7.-)
    Language English
    Publishing date 2021-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E20-10-0631
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  9. Article ; Online: A sugar phosphatase regulates the methylerythritol phosphate (MEP) pathway in malaria parasites.

    Guggisberg, Ann M / Park, Jooyoung / Edwards, Rachel L / Kelly, Megan L / Hodge, Dana M / Tolia, Niraj H / Odom, Audrey R

    Nature communications

    2014  Volume 5, Page(s) 4467

    Abstract: Isoprenoid biosynthesis through the methylerythritol phosphate (MEP) pathway generates commercially important products and is a target for antimicrobial drug development. MEP pathway regulation is poorly understood in microorganisms. Here we employ a ... ...

    Abstract Isoprenoid biosynthesis through the methylerythritol phosphate (MEP) pathway generates commercially important products and is a target for antimicrobial drug development. MEP pathway regulation is poorly understood in microorganisms. Here we employ a forward genetics approach to understand MEP pathway regulation in the malaria parasite, Plasmodium falciparum. The antimalarial fosmidomycin inhibits the MEP pathway enzyme deoxyxylulose 5-phosphate reductoisomerase (DXR). Fosmidomycin-resistant P. falciparum are enriched for changes in the PF3D7_1033400 locus (hereafter referred to as PfHAD1), encoding a homologue of haloacid dehalogenase (HAD)-like sugar phosphatases. We describe the structural basis for loss-of-function PfHAD1 alleles and find that PfHAD1 dephosphorylates a variety of sugar phosphates, including glycolytic intermediates. Loss of PfHAD1 is required for fosmidomycin resistance. Parasites lacking PfHAD1 have increased MEP pathway metabolites, particularly the DXR substrate, deoxyxylulose 5-phosphate. PfHAD1 therefore controls substrate availability to the MEP pathway. Because PfHAD1 has homologues in plants and bacteria, other HAD proteins may be MEP pathway regulators.
    MeSH term(s) Aldose-Ketose Isomerases/antagonists & inhibitors ; Aldose-Ketose Isomerases/metabolism ; Antimalarials/pharmacology ; Catalytic Domain ; Cytoplasm/metabolism ; Drug Resistance ; Erythritol/analogs & derivatives ; Erythritol/metabolism ; Fosfomycin/analogs & derivatives ; Fosfomycin/pharmacology ; Genetic Complementation Test ; Phosphoric Monoester Hydrolases/chemistry ; Phosphoric Monoester Hydrolases/genetics ; Phosphoric Monoester Hydrolases/metabolism ; Plasmodium falciparum/drug effects ; Plasmodium falciparum/genetics ; Plasmodium falciparum/metabolism ; Protein Conformation ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Sugar Phosphates/metabolism ; Xylose/analogs & derivatives ; Xylose/metabolism
    Chemical Substances 2-C-methylerythritol 4-phosphate ; Antimalarials ; Protozoan Proteins ; Sugar Phosphates ; deoxyxylulose phosphate ; Fosfomycin (2N81MY12TE) ; fosmidomycin (5829E3D9I9) ; Xylose (A1TA934AKO) ; 1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC 1.1.1.267) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; sugar-phosphatase (EC 3.1.3.23) ; Aldose-Ketose Isomerases (EC 5.3.1.-) ; Erythritol (RA96B954X6)
    Language English
    Publishing date 2014-07-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms5467
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  10. Article ; Online: Synthesis, characterization, and biological activity of poly(arginine)-derived cancer-targeting peptides in HepG2 liver cancer cells.

    Joseph, Stesha C / Blackman, Brittany A / Kelly, Megan L / Phillips, Mariana / Beaury, Michael W / Martinez, Ivonne / Parronchi, Christopher J / Bitsaktsis, Constantine / Blake, Allan D / Sabatino, David

    Journal of peptide science : an official publication of the European Peptide Society

    2014  Volume 20, Issue 9, Page(s) 736–745

    Abstract: The solid-phase synthesis, structural characterization, and biological evaluation of a small library of cancer-targeting peptides have been determined in HepG2 hepatoblastoma cells. These peptides are based on the highly specific Pep42 motif, which has ... ...

    Abstract The solid-phase synthesis, structural characterization, and biological evaluation of a small library of cancer-targeting peptides have been determined in HepG2 hepatoblastoma cells. These peptides are based on the highly specific Pep42 motif, which has been shown to target the glucose-regulated protein 78 receptors overexpressed and exclusively localized on the cell surface of tumors. In this study, Pep42 was designed to contain varying lengths (3-12) of poly(arginine) sequences to assess their influence on peptide structure and biology. Peptides were effectively synthesized by 9-fluorenylmethoxycarbonyl-based solid-phase peptide synthesis, in which the use of a poly(ethylene glycol) resin provided good yields (14-46%) and crude purities >95% as analyzed by liquid chromatography-mass spectrometry. Peptide structure and biophysical properties were investigated using circular dichroism spectroscopy. Interestingly, peptides displayed secondary structures that were contingent on solvent and length of the poly(arginine) sequences. Peptides exhibited helical and turn conformations, while retaining significant thermal stability. Structure-activity relationship studies conducted by flow cytometry and confocal microscopy revealed that the poly(arginine) derived Pep42 sequences maintained glucose-regulated protein 78 binding on HepG2 cells while exhibiting cell translocation activity that was contingent on the length of the poly(arginine) strand. In single dose (0.15 mM) and dose-response (0-1.5 mM) cell viability assays, peptides were found to be nontoxic in human HepG2 liver cancer cells, illustrating their potential as safe cancer-targeting delivery agents.
    MeSH term(s) Carcinoma, Hepatocellular/drug therapy ; Carcinoma, Hepatocellular/metabolism ; Carcinoma, Hepatocellular/pathology ; Cell-Penetrating Peptides/chemical synthesis ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/pharmacology ; Drug Delivery Systems/methods ; Heat-Shock Proteins/metabolism ; Hep G2 Cells ; Humans ; Liver Neoplasms/drug therapy ; Liver Neoplasms/metabolism ; Liver Neoplasms/pathology ; Neoplasm Proteins/metabolism ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/pharmacology ; Protein Binding ; Structure-Activity Relationship
    Chemical Substances Cell-Penetrating Peptides ; Heat-Shock Proteins ; Neoplasm Proteins ; Peptides ; molecular chaperone GRP78 ; polyarginine (25212-18-4)
    Language English
    Publishing date 2014-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 1234416-3
    ISSN 1099-1387 ; 1075-2617
    ISSN (online) 1099-1387
    ISSN 1075-2617
    DOI 10.1002/psc.2665
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