15 results on '"Ngambenjawong C"'
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2. Layer-by-layer nanocoating of chlorophene-loaded polymeric micelles on silicone catheters
- Author
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Ngambenjawong, C., primary, Phuengkham, H., additional, Theerasilp, M., additional, and Nasongkla, N., additional
- Published
- 2012
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3. Plasmon resonance tuning of gold and silver nanoparticle-insulator multilayered composite structures for optical filters
- Author
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Kitsomboonloha, R., primary, Ngambenjawong, C., additional, Mohammed, W.S., additional, Chaudhari, M.B., additional, Hornyak, G.L., additional, and Dutta, J., additional
- Published
- 2011
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4. CRISPR-Cas-amplified urinary biomarkers for multiplexed and portable cancer diagnostics.
- Author
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Hao L, Zhao RT, Welch NL, Tan EKW, Zhong Q, Harzallah NS, Ngambenjawong C, Ko H, Fleming HE, Sabeti PC, and Bhatia SN
- Subjects
- Humans, Animals, Mice, CRISPR-Cas Systems genetics, DNA, Biomarkers, Tumor Microenvironment, Neoplasms diagnosis, Neoplasms genetics, Nucleic Acids
- Abstract
Synthetic biomarkers, bioengineered sensors that generate molecular reporters in diseased microenvironments, represent an emerging paradigm in precision diagnostics. Despite the utility of DNA barcodes as a multiplexing tool, their susceptibility to nucleases in vivo has limited their utility. Here we exploit chemically stabilized nucleic acids to multiplex synthetic biomarkers and produce diagnostic signals in biofluids that can be 'read out' via CRISPR nucleases. The strategy relies on microenvironmental endopeptidase to trigger the release of nucleic acid barcodes and polymerase-amplification-free, CRISPR-Cas-mediated barcode detection in unprocessed urine. Our data suggest that DNA-encoded nanosensors can non-invasively detect and differentiate disease states in transplanted and autochthonous murine cancer models. We also demonstrate that CRISPR-Cas amplification can be harnessed to convert the readout to a point-of-care paper diagnostic tool. Finally, we employ a microfluidic platform for densely multiplexed, CRISPR-mediated DNA barcode readout that can potentially evaluate complex human diseases rapidly and guide therapeutic decisions., (© 2023. The Author(s).)
- Published
- 2023
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5. Conditional Antimicrobial Peptide Therapeutics.
- Author
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Ngambenjawong C, Chan LW, Fleming HE, and Bhatia SN
- Subjects
- Animals, Mice, Albumins, Peptide Hydrolases, Anti-Bacterial Agents, Antimicrobial Peptides therapeutic use
- Abstract
Antimicrobial peptides (AMPs) constitute a promising class of alternatives to antibiotics to curb antimicrobial resistance. Nonetheless, their utility as a systemic agent is hampered by short circulation time and toxicity. Infection sites, analogous to tumors, harbor an aberrant microenvironment that has the potential to be exploited to develop conditionally activated therapeutics with an improved therapeutic index. In particular, we identified strategies to prolong systemic circulation of small, cationic AMPs in a mouse model of bacterial pneumonia. Specifically, we report an albumin-binding domain (ABD)-AMP conjugate as a long-circulating conditional AMP therapeutic with a masked activity that can be liberated by proteases in the infected tissue microenvironment. Our systemically administered conjugate enhanced the pulmonary delivery of active AMP while also reducing AMP exposure to other off-target organs. Importantly, this reduction in off-target exposure improved the safety profile of the AMP. The framework we present can be generalized to quantify and optimize the performance of this emerging class of conditional therapeutics.
- Published
- 2022
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6. Selective Permeabilization of Gram-Negative Bacterial Membranes Using Multivalent Peptide Constructs for Antibiotic Sensitization.
- Author
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Chan LW, Hern KE, Ngambenjawong C, Lee K, Kwon EJ, Hung DT, and Bhatia SN
- Subjects
- Microbial Sensitivity Tests, Rifampin, Anti-Bacterial Agents pharmacology, Gram-Negative Bacteria
- Abstract
The drug-impermeable bacterial membrane in Gram-negative pathogens limits antibiotic access to intracellular drug targets. To expand our rapidly waning antibiotic arsenal, one approach is to improve the intracellular delivery of drugs with historically poor accumulation in Gram-negative bacteria. To do so, we engineered macromolecular potentiators to permeabilize the Gram-negative membrane to facilitate drug influx. Potentiators, known as WD40, were synthesized by grafting multiple copies of a cationic α-helical antimicrobial peptide, WLBU2, onto a dextran polymer scaffold. WD40 enabled drug uptake in the model pathogen P. aeruginosa , a capability that was not observed with unmodified WLBU2 peptide. WD40 was able to reduce minimum inhibitory concentrations of a drug panel by up to 3 orders of magnitude. Hydrophobic and highly three-dimensional antibiotics exhibited the greatest potentiation. Antibiotic activity was potentiated in several clinical strains and resulted in sensitization of drug-resistant strains to rifampin, a drug not previously used for Gram-negative infections.
- Published
- 2021
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7. Glomerular disease augments kidney accumulation of synthetic anionic polymers.
- Author
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Liu GW, Prossnitz AN, Eng DG, Cheng Y, Subrahmanyam N, Pippin JW, Lamm RJ, Ngambenjawong C, Ghandehari H, Shankland SJ, and Pun SH
- Subjects
- Animals, Anions, Glomerulosclerosis, Focal Segmental metabolism, Glomerulosclerosis, Focal Segmental pathology, Humans, Kidney Tubules, Proximal metabolism, Kidney Tubules, Proximal pathology, Mice, Molecular Weight, Polymers chemical synthesis, Polymers chemistry, Tissue Distribution, Kidney Diseases metabolism, Kidney Diseases pathology, Kidney Glomerulus metabolism, Kidney Glomerulus pathology, Polymers metabolism
- Abstract
Polymeric drug carriers can alter the pharmacokinetics of their drug cargoes, thereby improving drug therapeutic index and reducing side effects. Understanding and controlling polymer properties that drive tissue-specific accumulation is critical in engineering targeted drug delivery systems. For kidney disease applications, targeted drug delivery to renal cells that reside beyond the charge- and size-selective glomerular filtration barrier could have clinical potential. However, there are limited reports on polymer properties that might enhance kidney accumulation. Here, we studied the effects of molecular weight and charge on the in vivo kidney accumulation of polymers in health and disease. We synthesized a panel of well-defined polymers by atom transfer radical polymerization to answer several questions. First, the biodistribution of low molecular weight (23-27 kDa) polymers composed of various ratios of neutral:anionic monomers (1:0, 1:1, 1:4) in normal mice was determined. Then, highly anionic (1:4 monomer ratio) low molecular and high molecular weight (47 kDa) polymers were tested in both normal and experimental focal segmental glomerulosclerosis (FSGS) mice, a model that results in loss of glomerular filtration selectivity. Through these studies, we observed that kidney-specific polymer accumulation increases with anionic monomer content, but not molecular weight; experimental FSGS increases kidney accumulation of anionic polymers; and anionic polymers accumulate predominantly in proximal tubule cells, with some distribution in kidney glomeruli. These findings can be applied to the design of polymeric drug carriers to enhance or mitigate kidney accumulation., (Copyright © 2018 Elsevier Ltd. All rights reserved.)
- Published
- 2018
- Full Text
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8. Reversibly Switchable, pH-Dependent Peptide Ligand Binding via 3,5-Diiodotyrosine Substitutions.
- Author
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Ngambenjawong C, Sylvestre M, Gustafson HH, Pineda JMB, and Pun SH
- Subjects
- Drug Delivery Systems methods, Humans, Molecular Targeted Therapy methods, Diiodotyrosine metabolism, Hydrogen-Ion Concentration, Ligands, Macrophages metabolism, Peptides metabolism
- Abstract
Cell type-specific targeting ligands utilized in drug delivery applications typically recognize receptors that are overexpressed on the cells of interest. Nonetheless, these receptors may also be expressed, to varying extents, on off-target cells, contributing to unintended side effects. For the selectivity profile of targeting ligands in cancer therapy to be improved, stimuli-responsive masking of these ligands with acid-, redox-, or enzyme-cleavable molecules has been reported, whereby the targeting ligands are exposed in specific environments, e.g., acidic tumor hypoxia. One possible drawback of these systems lies in their one-time, permanent trigger, which enables the "demasked" ligands to bind off-target cells if released back into the systemic circulation. A promising strategy to address the aforementioned problem is to design ligands that show selective binding based on ionization state, which may be microenvironment-dependent. In this study, we report a systematic strategy to engineer low pH-selective targeting peptides using an M2 macrophage-targeting peptide (M2pep) as an example. 3,5-Diiodotyrosine mutagenesis into native tyrosine residues of M2pep confers pH-dependent binding behavior specific to acidic environment (pH 6) when the amino acid is protonated into the native tyrosine-like state. At physiological pH of 7.4, the hydroxyl group of 3,5-diiodotyrosine on the peptide is deprotonated leading to interruption of the peptide native binding property. Our engineered pH-responsive M2pep (Ac-Y-Î-Î) binds target M2 macrophages more selectively at pH 6 than at pH 7.4. In addition, 3,5-diiodotyrosine substitutions also improve serum stability of the peptide. Finally, we demonstrate pH-dependent reversibility in target binding via a postbinding peptide elution study. The strategy presented here should be applicable for engineering pH-dependent functionality of other targeting peptides with potential applications in physiology-dependent in vivo targeting applications (e.g., targeting hypoxic tumor/inflammation) or in in vitro receptor identification.
- Published
- 2018
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9. A Facile Cyclization Method Improves Peptide Serum Stability and Confers Intrinsic Fluorescence.
- Author
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Ngambenjawong C, Gustafson HH, Sylvestre M, and Pun SH
- Subjects
- Animals, Cysteine chemistry, Female, Flow Cytometry methods, Fluorobenzenes chemistry, Mammary Neoplasms, Animal diagnostic imaging, Methods, Mice, Nitriles chemistry, Optical Imaging methods, Cyclization, Fluorescence, Peptides blood, Protein Stability
- Abstract
Peptides are a growing class of macromolecules used in pharmaceutics. The path toward the clinical use of candidate peptides involves sequence optimization and cyclization for stability and affinity. For internalized peptides, tagging is also often required for intracellular trafficking studies, although fluorophore conjugation has an impact on peptide binding, permeability, and localization. Herein, a strategy based on cysteine arylation with tetrafluoroterephthalonitrile (4F-2CN), which simultaneously cyclizes peptides and imparts fluorescence, is reported. The 4F-2CN cyclization of an M2 macrophage-targeting peptide yields, in a single step, a peptide with improved serum stability, intrinsic fluorescence, and increased binding affinity. In a murine breast cancer model, it is demonstrated that the intrinsic fluorescence from the cyclized peptide is sufficient for monitoring biodistribution by whole-organ fluorescence imaging and cell internalization by flow cytometry., (© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Published
- 2017
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10. Multivalent polymers displaying M2 macrophage-targeting peptides improve target binding avidity and serum stability.
- Author
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Ngambenjawong C and Pun SH
- Abstract
Tumor-associated macrophages (TAMs) display a spectrum of phenotypes ranging from pro-tumoral/anti-inflammatory "M2-like" to anti-tumoral/pro-inflammatory "M1-like" subtypes and, consequently, high intratumoral M2-to-M1 ratios are typically indicative of poor disease prognosis. Cancer immunotherapies that selectively modulate M2-like TAMs, enabling reversal of the M2-to-M1 ratio, represent a promising anti-cancer intervention but are difficult to implement due to the lack of effective targeting systems. In this study, we report the development of high avidity, M2 macrophage-selective targeted drug delivery platforms based on M2 macrophage-targeting peptides (M2pep) grafted onto poly( N -(2-hydroxypropyl) methacrylamide). Furthermore, these M2pep-grafted polymers also exhibit improved serum stability along with M2 macrophage-selective toxicity.
- Published
- 2017
- Full Text
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11. Progress in tumor-associated macrophage (TAM)-targeted therapeutics.
- Author
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Ngambenjawong C, Gustafson HH, and Pun SH
- Subjects
- Animals, Humans, Macrophages immunology, Neoplasms blood supply, Neoplasms pathology, Tumor Microenvironment immunology, Immunotherapy methods, Macrophages drug effects, Neoplasms immunology, Neoplasms therapy, Tumor Microenvironment drug effects
- Abstract
As an essential innate immune population for maintaining body homeostasis and warding off foreign pathogens, macrophages display high plasticity and perform diverse supportive functions specialized to different tissue compartments. Consequently, aberrance in macrophage functions contributes substantially to progression of several diseases including cancer, fibrosis, and diabetes. In the context of cancer, tumor-associated macrophages (TAMs) in tumor microenvironment (TME) typically promote cancer cell proliferation, immunosuppression, and angiogenesis in support of tumor growth and metastasis. Oftentimes, the abundance of TAMs in tumor is correlated with poor disease prognosis. Hence, significant attention has been drawn towards development of cancer immunotherapies targeting these TAMs; either depleting them from tumor, blocking their pro-tumoral functions, or restoring their immunostimulatory/tumoricidal properties. This review aims to introduce readers to various aspects in development and evaluation of TAM-targeted therapeutics in pre-clinical and clinical stages., (Copyright © 2017 Elsevier B.V. All rights reserved.)
- Published
- 2017
- Full Text
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12. Engineering an Affinity-Enhanced Peptide through Optimization of Cyclization Chemistry.
- Author
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Ngambenjawong C, Pineda JM, and Pun SH
- Subjects
- Animals, Azides chemistry, Biotin chemistry, Chemistry Techniques, Synthetic, Circular Dichroism, Macrophages metabolism, Mice, Peptides blood, Peptides chemical synthesis, Protein Engineering methods, Protein Stability, Peptides chemistry, Peptides metabolism
- Abstract
Peptide cyclization is a strategy used to improve stability and activity of peptides. The most commonly used cyclization method is disulfide bridge formation of cysteine-containing peptides, as is typically found in nature. Over the years, an increasing number of alternative chemistries for peptide cyclization with improved efficiency, kinetics, orthogonality, and stability have been reported. However, there has been less appreciation for the opportunity to fine-tune peptide activity via the diverse chemical entities introduced at the site of linkage by different cyclization strategies. Here, we demonstrate how cyclization optimization of an M2 "anti-inflammatory" macrophage-binding peptide (M2pep) resulted in a significant increase in binding affinity of the optimized analog to M2 macrophages while maintaining binding selectivity compared to M1 "pro-inflammatory" macrophages. In this study, we report synthesis and evaluation of four cyclic M2pep(RY) analogs with diverse cyclization strategies: (1) Asp-[amide]-Lys, (2) azido-Lys-[triazole(copper(I)-catalyzed alkyne-azide cycloaddition (CuAAC))]-propargyl-Gly, (3) Cys-[decafluorobiphenyl (DFBP)]-Cys, and (4) Cys-[decafluorobiphenyl sulfone (DFS)]-Cys, whereby the chemical entity or linker at the linkage site is shown in the square bracket and is between the residues involved in cyclization. These peptides are compared to a disulfide-cyclized M2pep(RY) that we previously reported as a serum-stable, affinity-enhanced analog to the original linear M2pep. DFBP-cyclized M2pep(RY) exhibits the highest binding activity to M2 macrophages with apparent dissociation constant (K
D ) about 2.03 μM compared to 36.3 μM for the original disulfide-cyclized M2pep(RY) and 220 μM for the original linear peptide. DFS-cyclized M2pep(RY) also binds more strongly than the original cyclized analog, whereas amide- and triazole-cyclized M2pep(RY) analogs bind less strongly. We verified that DFBP alone has negligible binding to M2 macrophages and the incorporation of diphenylalanine to the original sequence improves binding activity at the expense of solubility and increased toxicity. In conclusion, we report development of cyclic M2pep(RY) analogs with diverse cyclization strategies leading to the discovery of DFBP-cyclized M2pep(RY) with enhanced M2 macrophage-binding activity.- Published
- 2016
- Full Text
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13. Serum Stability and Affinity Optimization of an M2 Macrophage-Targeting Peptide (M2pep).
- Author
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Ngambenjawong C, Gustafson HH, Pineda JM, Kacherovsky NA, Cieslewicz M, and Pun SH
- Subjects
- Animals, Antineoplastic Agents administration & dosage, Breast Neoplasms drug therapy, Cell Cycle Proteins, Colonic Neoplasms drug therapy, Disease Models, Animal, Drug Carriers chemistry, Macrophages metabolism, Mice, Peptides, Cyclic chemistry, Protein Stability, Proteolysis, Antineoplastic Agents pharmacokinetics, Antineoplastic Agents pharmacology, Drug Carriers metabolism, Macrophages drug effects, Peptides, Cyclic metabolism, Serum chemistry
- Abstract
Tumor associated macrophages (TAMs) are a major stromal component of the tumor microenvironment in several cancers. TAMs are a potential target for adjuvant cancer therapies due to their established roles in promoting proliferation of cancer cells, angiogenesis, and metastasis. We previously discovered an M2 macrophage-targeting peptide (M2pep) which was successfully used to target and deliver a pro-apoptotic KLA peptide to M2-like TAMs in a CT-26 colon carcinoma model. However, the effectiveness of in vivo TAM-targeting using M2pep is limited by its poor serum stability and low binding affinity. In this study, we synthesized M2pep derivatives with the goals of increasing serum stability and binding affinity. Serum stability evaluation of M2pepBiotin confirmed its rapid degradation attributed to exolytic cleavage from the N-terminus and endolytic cleavages at the W10/W11 and S16/K17 sites. N-terminal acetylation of M2pepBiotin protected the peptide against the exolytic degradation while W10w and K(17,18,19)k substitutions were able to effectively protect endolytic degradation at their respective cleavage sites. However, no tested amino acid changes at the W10 position resulted in both protease resistance at that site and retention of binding activity. Therefore, cyclization of M2pep was investigated. Cyclized M2pep better resisted serum degradation without compromising binding activity to M2 macrophages. During the serum stability optimization process, we also discovered that K9R and W10Y substitutions significantly enhanced binding affinity of M2pep. In an in vitro binding study of different M2pep analogs pre-incubated in mouse serum, cyclic M2pep with K9R and W10Y modifications (cyclic M2pep(RY)) retained the highest binding activity to M2 macrophages over time due to its improved serum stability. Finally, we evaluated the in vivo accumulation of sulfo-Cy5-labeled M2pep and cyclic M2pep(RY) in both the CT-26 and 4T1 breast carcinoma models. Cyclic M2pep(RY) outperformed M2pep in both tumor localization and selective accumulation in M2-like TAMs. In conclusion, we report cyclic M2pep(RY) as our lead M2pep analog with improved serum stability and M2 macrophage-binding activity. Its enhanced utility as an in vivo M2-like-TAM-targeting agent was demonstrated in two tumor models, and is expected to be applicable for other tumor models or in models of M2 macrophage-related diseases.
- Published
- 2016
- Full Text
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14. Synthesis and evaluation of multivalent M2pep peptides for targeting alternatively activated M2 macrophages.
- Author
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Ngambenjawong C, Cieslewicz M, Schellinger JG, and Pun SH
- Subjects
- Animals, Antineoplastic Agents administration & dosage, Antineoplastic Agents therapeutic use, Apoptosis drug effects, Biotin chemistry, Bone Marrow Cells drug effects, Cell Line, Tumor, Cell Survival drug effects, Drug Delivery Systems, Humans, Mice, Mice, Inbred C57BL, Tumor Microenvironment, Macrophages drug effects, Peptides chemical synthesis, Peptides pharmacology
- Abstract
The tumor microenvironment in the majority of cancers is known to favor polarization of tumor-associated macrophages (TAMs) to alternatively activated M2 phenotype, promoting disease progression and reducing patient survival. Effective therapy targeting this M2 macrophage population is thus a promising adjuvant to approved cancer therapies. One of the challenges in targeting M2-like TAMs is a lack of high affinity targeting ligand with good selectivity over anti-tumor M1-like TAMs. We have previously identified an M2 macrophage-targeting peptide (M2pep) that binds preferentially to murine M2 macrophages and M2-like TAMs. A fusion peptide of M2pep with pro-apoptotic peptide KLA (M2pepKLA) was further used to reduce TAM population in vivo but high concentrations and frequent dosing were required due to low binding affinity of M2pep for M2 macrophage. The goal of this study was to develop more potent TAM depletion constructs by increasing the valency of both the M2pep targeting and KLA drug domains. Divalent and tetravalent displays of M2pep ([M2pep]2-Biotin and [M2pep]4-Biotin) were synthesized and evaluated for improvement in binding avidity to the murine macrophages. High avidity and selective binding of [M2pep]2-Biotin to M2 macrophages were achieved with at least 10-fold lower concentration than required for monovalent M2pep activity. Increasing M2pep valency to four, however, resulted in a reduction in both binding activity and selectivity. Surprisingly, both divalent and tetravalent M2pep, without conjugation of any cytotoxic drug cargo, exhibited M2 macrophage-selective toxicity not observed in monovalent M2pep treatment. We next synthesized divalent M2pep with monovalent and divalent KLA ([M2pep]2-[KLA] and [M2pep]2-[KLA]2) to evaluate its enhanced potency compared to M2pepKLA. While both constructs were significantly more toxic than M2pepKLA to primary, bone marrow-derived M2 macrophage, desired selectivity was retained only with [M2pep]2-[KLA]. Finally, we evaluated all multivalent M2pep and M2pepKLA analogs using a syngeneic CT-26 tumor cell suspension. In this setting, [M2pep]4-Biotin and [M2pep]2-[KLA]2 exhibited selective toxicity to both M2-like TAMs and malignant cells but not to M1-like TAMs. Therefore, these constructs are promising anti-cancer constructs with dual-modality mechanisms: malignant cell killing and TAM-based immunomodulation., (Copyright © 2016 Elsevier B.V. All rights reserved.)
- Published
- 2016
- Full Text
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15. Multivalent display of pendant pro-apoptotic peptides increases cytotoxic activity.
- Author
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Chu DS, Bocek MJ, Shi J, Ta A, Ngambenjawong C, Rostomily RC, and Pun SH
- Subjects
- Animals, Antineoplastic Agents chemistry, Antineoplastic Agents metabolism, Carrier Proteins, Cell Survival drug effects, Chemistry, Pharmaceutical, Dose-Response Relationship, Drug, HeLa Cells, Humans, Inhibitory Concentration 50, Intercellular Signaling Peptides and Proteins, Ligands, Mice, Mitochondrial Proteins metabolism, Neoplasms metabolism, Neoplasms pathology, Oligopeptides chemistry, Oligopeptides metabolism, Peptides chemistry, Peptides metabolism, Polymerization, Technology, Pharmaceutical methods, Antineoplastic Agents pharmacology, Apoptosis drug effects, Drug Carriers, Methacrylates chemistry, Neoplasms drug therapy, Oligopeptides pharmacology, Peptides pharmacology
- Abstract
Several cationic antimicrobial peptides have been investigated as potential anti-cancer drugs due to their demonstrated selective toxicity towards cancer cells relative to normal cells. For example, intracellular delivery of KLA, a pro-apoptotic peptide, results in toxicity against a variety of cancer cell lines; however, the relatively low activity and small size lead to rapid renal excretion when applied in vivo, limiting its therapeutic potential. In this work, apoptotic peptide-polymer hybrid materials were developed to increase apoptotic peptide activity via multivalent display. Multivalent peptide materials were prepared with comb-like structure by RAFT copolymerization of peptide macromonomers with N-(2-hydroxypropyl) methacrylamide (HPMA). Polymers displayed a GKRK peptide sequence for targeting p32, a protein often overexpressed on the surface of cancer cells, either fused with or as a comonomer to a KLA macromonomer. In three tested cancer cell lines, apoptotic polymers were significantly more cytotoxic than free peptides as evidenced by an order of magnitude decrease in IC50 values for the polymers compared to free peptide. The uptake efficiency and intracellular trafficking of one polymer construct was determined by radiolabeling and subcellular fractionation. Despite their more potent cytotoxic profile, polymeric KLA constructs have poor cellular uptake efficiency (<1%). A significant fraction (20%) of internalized constructs localize with intact mitochondrial fractions. In an effort to increase cellular uptake, polymer amines were converted to guanidines by reaction with O-methylisourea. Guanidinylated polymers disrupted function of isolated mitochondria more than their lysine-based analogs, but overall toxicity was decreased, likely due to inefficient mitochondrial trafficking. Thus, while multivalent KLA polymers are more potent than KLA peptides, these materials can be substantially improved by designing next generation materials with improved cellular internalization and mitochondrial targeting efficiency., (Copyright © 2015 Elsevier B.V. All rights reserved.)
- Published
- 2015
- Full Text
- View/download PDF
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