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[PMID]: 29524730
[Au] Autor:Palacios M; Tampe R; Del Campo M; Zhong TY; López MN; Salazar-Onfray F; Becker MI
[Ad] Address:Fundación Ciencia y Tecnología para el Desarrollo (FUCITED), Avenida Eduardo Castillo Velasco 2902, Santiago 7750269, Chile.
[Ti] Title:Antitumor activity and carrier properties of novel hemocyanins coupled to a mimotope of GD2 ganglioside.
[So] Source:Eur J Med Chem;150:74-86, 2018 Feb 27.
[Is] ISSN:1768-3254
[Cp] Country of publication:France
[La] Language:eng
[Ab] Abstract:Conjugation to carrier proteins is a way to improve the immunogenicity of peptides. Such is the case for peptides mimicking carbohydrate tumor-associated antigens in cancer vaccine development. The most used protein for this purpose is the keyhole limpet hemocyanin (KLH) from Megathura crenulata. Its limited bioavailability has prompted interest in finding new candidates; nevertheless, it is not known whether other hemocyanins might be equally efficient as carrier of carbohydrate peptide mimotopes to promotes anti-tumor responses. Here, we evaluated the carrier and antitumor activity of novel hemocyanins with documented immunogenicity obtained from Concholepas concholepas (CCH) and Fissurella latimarginata (FLH), coupled through sulfo-SMCC to P10, a mimetic peptide of GD2, the major ganglioside constituent of neuroectodermal tumors, and incorporating AddaVax as an adjuvant. The humoral immune responses of mice showed that CCH-P10 and FLH-P10 conjugates elicited specific IgM and IgG antibodies against P10 mimotope, similar to those obtained with KLH-P10, which was used as a positive control. The CCH-P10 and FLH-P10 antisera, exhibited cross-reactivity with murine and human melanoma cells, like anti-CCH and anti-FLH sera suggesting a cross-reaction of CCH and FLH glycosylations with carbohydrate epitopes on the tumor cell surfaces, similar to the KLH antisera. When mice were primed with each hemocyanin-P10 and challenged with melanoma cells, better antitumor effects were observed for FLH-P10 than for CCH-P10 and, as for KLH-P10, irrespective of conjugation. These data demonstrate that CCH and FLH are useful carriers of carbohydrate mimotopes; however, the best antitumor activity of FLH preparations, indicate that is a suitable candidate for further cancer vaccines research.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 483246 MEDLINE  
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[PMID]: 29524585
[Au] Autor:Shartouny JR; Jacob J
[Ad] Address:Emory University, 954 Gatewood Rd., Atlanta, GA 30329, Georgia.
[Ti] Title:Mining the tree of life: Host defense peptides as antiviral therapeutics.
[So] Source:Semin Cell Dev Biol;, 2018 Mar 07.
[Is] ISSN:1096-3634
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Discovering new therapeutics for human viral diseases is important for combatting emerging infectious viruses and omnipresent circulating viruses as well as those that can become resistant to the drugs we currently have available. The innate host defense peptide (HDP) repertoire present in animals is a wealth of potential antimicrobial agents that could be mined to meet these needs. While much of the body of research regarding HDPs is in the context of bacteria, there is increasing evidence that they can be an effective source for antivirals. Peptides can be identified in a number of ways, including eco-conservation-minded approaches. Those shown to have antiviral properties can be modified to exhibit desired properties as the relationship between structure and function is elucidated and then developed into therapeutics for human use. This review looks at the discovery and therapeutic potential of HDPs for human viral infections.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  3 / 483246 MEDLINE  
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[PMID]: 29524563
[Au] Autor:Asferg CL; Nielsen SJ; Andersen UB; Linneberg A; Goetze JP; Jeppesen JL
[Ad] Address:Department of Clinical Physiology, Rigshospitalet Glostrup, University of Copenhagen, Glostrup, Denmark. Electronic address: c.asferg@gmail.com.
[Ti] Title:Serum proatrial natriuretic peptide concentrations during oral glucose-induced acute hyperinsulinemia in lean and obese men.
[So] Source:Peptides;, 2018 Mar 07.
[Is] ISSN:1873-5169
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Atrial natriuretic peptide (ANP) is primarily seen as a hormone involved in salt and water homeostasis and blood pressure regulation. Evidence supports a link between metabolism and ANP. Circulating ANP concentrations are low in obese individuals with insulin resistance and hyperinsulinemia. The dynamic relationship between insulin and ANP has been sparsely studied. We therefore measured circulating concentrations of midregional proatrial natriuretic peptide (MR-proANP), a stable marker of ANP secretion, and insulin in lean and obese men during an oral glucose challenge. One hundred and three obese men (body mass index (BMI) ≥30.0 kg/m ) were compared with 27 lean men (BMI = 20.0-24.9 kg/m ). During a 75 gram oral glucose challenge, circulating concentrations of MR-proANP and insulin were measured at baseline and every half hour for 2 hours. Fasting MR-proANP concentrations were lower in the obese men as compared with the lean men (median (interquartile range): 51.2 (38.7-64.7) pmol/L vs. 69.3 (54.3-82.9) pmol/L, P = 0.002). During the oral glucose challenge, serum MR-proANP concentrations fell steadily in the obese men (P < 0.0001), whereas there was no significant fall in the lean men (P = 0.14). However, the time-course curves of MR-proANP did not display a clear reciprocal relation to the time-course curves of insulin. Adjusted for age, the area under curve (AUC) for MR-proANP was inversely correlated with AUC for insulin (r = -0.38, P < 0.0001). In conclusion, during an oral glucose challenge, serum MR-proANP concentrations drop significantly in obese individuals, but the time-course curves of MR-proANP do not display a reciprocal relationship to the time-course curves of insulin.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  4 / 483246 MEDLINE  
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[PMID]: 29524562
[Au] Autor:Zera T; Przybylski J; Grygorowicz T; Kasarello K; Podobinska M; Mirowska-Guzel D; Cudnoch-Jedrzejewska A
[Ad] Address:Department of Experimental and Clinical Physiology, Laboratory of Centre for Preclinical Research, the Medical University of Warsaw, Banacha 1B, 02-097 Warsaw, Poland. Electronic address: tzera@wum.edu.pl.
[Ti] Title:Vasopressin V1a receptors are present in the carotid body and contribute to the control of breathing in male Sprague-Dawley rats.
[So] Source:Peptides;, 2018 Mar 07.
[Is] ISSN:1873-5169
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Vasopressin (AVP) maintains body homeostasis by regulating water balance, cardiovascular system and stress response. AVP inhibits breathing through central vasopressin 1a receptors (V1aRs). Chemoreceptors within carotid bodies (CBs) detect chemical and hormonal signals in the bloodstream and provide sensory input to respiratory and cardiovascular centers of the brainstem. In the study we investigated if CBs contain V1aRs and how the receptors are involved in the regulation of ventilation by AVP. We first immunostained CBs for V1aRs and tyrosine hydroxylase, a marker of chemoreceptor type I (glomus) cells. In urethane-anesthetized adult Sprague-Dawley male rats, we then measured hemodynamic and respiratory responses to systemic (intravenous) or local (carotid artery) administration of AVP prior and after systemic blockade of V1aRs. Immunostaining of CBs showed colocalization of V1aRs and tyrosine hydroxylase within glomus cells. Systemic administration of AVP increased mean arterial blood pressure (MABP) and decreased respiratory rate (RR) and minute ventilation (MV). Local administration of AVP increased MV and RR without significant changes in MABP or heart rate. Pretreatment with V1aR antagonist abolished responses to local and intravenous AVP administration. Our findings show that chemosensory cells within CBs express V1aRs and that local stimulation of the CB with AVP increases ventilation, which is contrary to systemic effects of AVP manifested by decreased ventilation. The responses are mediated by V1aRs, as blockade of the receptors prevents changes in ventilation. We hypothesize that excitatory effects of AVP within the CB provide a counterbalancing mechanism for the inhibitory effects of systemically acting AVP on the respiration.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  5 / 483246 MEDLINE  
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[PMID]: 29524561
[Au] Autor:Timmermans JP
[Ad] Address:Laboratory of Cell Biology & Histology, Department of Veterinary Sciences, University of Antwerp, Universiteitsplein 1, BE 2610 Wilrijk, Belgium. Electronic address: jean-pierre.timmermans@uantwerpen.be.
[Ti] Title:Need for more holistic therapeutic and management strategies to understand the causal or correlative link of the Aß amyloid pathway with Alzheimer's disease for a more efficiënt treatment.
[So] Source:Peptides;, 2018 Mar 07.
[Is] ISSN:1873-5169
[Cp] Country of publication:United States
[La] Language:eng
[Pt] Publication type:EDITORIAL
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  6 / 483246 MEDLINE  
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[PMID]: 29515106
[Au] Autor:Xie X; Zhou W; Hu Y; Chen Y; Zhang H; Li Y
[Ad] Address:Department of Hematology, Zhujiang Hospital, Southern Medical University, No. 253 GongyeDadaoZhong, Guangzhou, Guangdong, 510282, China.
[Ti] Title:A dual-function epidermal growth factor receptor pathway substrate 8 (Eps8)-derived peptide exhibits a potent cytotoxic T lymphocyte-activating effect and a specific inhibitory activity.
[So] Source:Cell Death Dis;9(3):379, 2018 Mar 07.
[Is] ISSN:2041-4889
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The identification and characterization of tumor-associated antigens (TAAs) that generate specific cytotoxic T lymphocytes (CTLs) are vital to the development of cancer immunotherapy. The epidermal growth factor receptor (EGFR) pathway substrate 8 gene (Eps8) is involved in regulating cancer progression and might be an ideal antigen. In this study, we searched for novel human leukocyte antigen (HLA)-A*2402-restricted epitopes derived from the Eps8 protein via the HLA-binding prediction algorithm. Among four candidates, peptides 327 (EFLDCFQKF), 534 (KYAKSKYDF) and 755 (LFSLNKDEL) induced peptide-specific CTLs to secrete higher levels of interferon-gamma (IFN-γ) and showed enhanced cytotoxic activity against malignant cancer cells. Our results demonstrated that peptide-specific CTLs showed effective antitumor responses, including upregulation of interleukin-2 (IL-2), tumor necrosis factor-alpha (TNF-α), granzyme B and perforin. Treatment with peptide-sensitized peripheral blood mononuclear cells (PBMCs) significantly reduced the tumor growth in vivo compared with the non-peptide-sensitized PBMC treatment. Importantly, our results indicated that peptide 327 may interfere with EGFR signaling by mechanistically disrupting Eps8/EGFR complex formation. We extended this observation that peptide 327 also suppressed the viability of cancer cells, blocked EGFR signal pathway and reduced the expression of downstream targets. Notably, conjugation of peptide 327 to the TAT sequence (TAT-327) resulted in potent antitumor activity and selective insertion into cancer cell membranes, where it adopted a punctate distribution. Furthermore, peptide 327 and TAT-327 displayed anticancer properties in xenograft models. Our results indicated that 327, 534 and 755 were novel HLA-A*2402-restricted epitopes from Eps8. By inhibiting the Eps8/EGFR interaction, peptide 327 and TAT-327 may serve as novel peptide inhibitors, which could provide an innovative approach for treating various cancers.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1038/s41419-018-0420-5

  7 / 483246 MEDLINE  
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[PMID]: 29511176
[Au] Autor:Piguet F; Ouldali H; Pastoriza-Gallego M; Manivet P; Pelta J; Oukhaled A
[Ad] Address:LAMBE UMR 8587, Université de Cergy-Pontoise, 95300, Pontoise, France. fabien.piguet@u-cergy.fr.
[Ti] Title:Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore.
[So] Source:Nat Commun;9(1):966, 2018 Mar 06.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:There are still unmet needs in finding new technologies for biomedical diagnostic and industrial applications. A technology allowing the analysis of size and sequence of short peptide molecules of only few molecular copies is still challenging. The fast, low-cost and label-free single-molecule nanopore technology could be an alternative for addressing these critical issues. Here, we demonstrate that the wild-type aerolysin nanopore enables the size-discrimination of several short uniformly charged homopeptides, mixed in solution, with a single amino acid resolution. Our system is very sensitive, allowing detecting and characterizing a few dozens of peptide impurities in a high purity commercial peptide sample, while conventional analysis techniques fail to do so.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1038/s41467-018-03418-2

  8 / 483246 MEDLINE  
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[PMID]: 29507109
[Au] Autor:Singh T; Fakiola M; Oommen J; Singh AP; Singh AK; Smith N; Chakravarty J; Sundar S; Blackwell JM
[Ad] Address:Institute of Medical Sciences, Banaras Hindu University, Varanasi OS 221 005, India.
[Ti] Title:Epitope-Binding Characteristics for Risk versus Protective DRB1 Alleles for Visceral Leishmaniasis.
[So] Source:J Immunol;, 2018 Mar 05.
[Is] ISSN:1550-6606
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:HLA-DRB1 is the major genetic risk factor for visceral leishmaniasis (VL). We used SNP2HLA to impute HLA-DRB1 alleles and SNPTEST to carry out association analyses in 889 human cases and 977 controls from India. NetMHCIIpan 2.1 was used to map epitopes and binding affinities across 49 vaccine candidates, as well as across peptide epitopes captured from dendritic cells treated with crude Ag and identified using mass spectrometry and alignment to amino acid sequences of a reference genome. Cytokines were measured in peptide-stimulated whole blood from 26 cured VL cases and eight endemic healthy controls. HLA-DRB1*1501 and DRB1*1404/DRB1*1301 were the most significant protective and risk alleles, respectively, with specific residues at aa positions 11 and 13 unique to protective alleles. We observed greater peptide promiscuity in sequence motifs for 9-mer core epitopes predicted to bind to risk (*1404/*1301) compared with protective (*1501) DRB1 alleles. There was a higher frequency of basic amino acids in DRB1*1404/*1301-specific epitopes compared with hydrophobic and polar amino acids in DRB1*1501-specific epitopes at anchor residues pocket 4 and pocket 6, which interact with residues at DRB1 positions 11 and 13. Cured VL patients made variable, but robust, IFN-γ, TNF, and IL-10 responses to 20-mer peptides based on captured epitopes, with peptides based on DRB1*1501-captured epitopes resulting in a higher proportion (odds ratio 2.23, 95% confidence interval 1.17-4.25, = 0.017) of patients with IFN-γ/IL-10 ratios > 2-fold compared with peptides based on DRB1*1301-captured epitopes. Our data provide insight into the molecular mechanisms underpinning the association of HLA-DRB1 alleles with risk versus protection in VL in humans.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:Publisher

  9 / 483246 MEDLINE  
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[PMID]: 29501398
[Au] Autor:Tang D; Xiao Z; Xu Y; Zeng J; Peng D; Liang S; Tang C; Liu Z
[Ad] Address:The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, 410081, China.
[Ti] Title:The peptide toxin δ-hexatoxin-MrIX inhibits fast inactivation of Na s in mouse cerebellar granule cells.
[So] Source:Peptides;102:47-53, 2018 Mar 06.
[Is] ISSN:1873-5169
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Spider venom is rich in peptide toxins that could be used to explore the structure and function of voltage-gated sodium channels (Na s). This study has characterized a 44-amino acid peptide toxin, δ-hexatoxin-MrIX (δ-HXTX-MrIX), from the venom of the spider Macrothele raveni. δ-hexatoxin-MrIX potently inhibited the fast inactivation of Na s in mouse cerebellar granule cells (CGCs) with an EC of 35.3 ±â€¯5.9 nM. The toxin shifted both the steady-state activation and the steady-state inactivation curves of CGC Na s to the hyperpolarized direction. δ-hexatoxin-MrIX also acted on Na 1.3 and Na 1.4 channels heterologously expressed in HEK293T cells, as well as on Na s in acutely isolated cockroach DUM neurons. However, the Na 1.5, Na 1.7 and Na 1.8 channels were resistant to δ-hexatoxin-MrIX. The toxin inhibited the fast inactivation of Na 1.3 and Na 1.4 with high affinity (EC values of 82.0 ±â€¯3.0 nM and 24.0 ±â€¯4.7 nM, respectively), but the saturating dose of toxin showed distinct efficacy on these two types of channels. δ-hexatoxin-MrIX is a peptide toxin acting on CGC Na s and could be used as a pharmacological tool to explore the role of Na s in granule cell maturation during cerebellum development.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  10 / 483246 MEDLINE  
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[PMID]: 29491361
[Au] Autor:Khodaparast L; Khodaparast L; Gallardo R; Louros NN; Michiels E; Ramakrishnan R; Ramakers M; Claes F; Young L; Shahrooei M; Wilkinson H; Desager M; Mengistu Tadesse W; Nilsson KPR; Hammarström P; Aertsen A; Carpentier S; Van Eldere J; Rousseau F; Schymkowitz J
[Ad] Address:Laboratory of Clinical Bacteriology and Mycology, Department of Microbiology and Immunology, KULeuven, Herestraat 49, 3000, Leuven, Belgium.
[Ti] Title:Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis.
[So] Source:Nat Commun;9(1):866, 2018 Feb 28.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Aggregation is a sequence-specific process, nucleated by short aggregation-prone regions (APRs) that can be exploited to induce aggregation of proteins containing the same APR. Here, we find that most APRs are unique within a proteome, but that a small minority of APRs occur in many proteins. When aggregation is nucleated in bacteria by such frequently occurring APRs, it leads to massive and lethal inclusion body formation containing a large number of proteins. Buildup of bacterial resistance against these peptides is slow. In addition, the approach is effective against drug-resistant clinical isolates of Escherichia coli and Acinetobacter baumannii, reducing bacterial load in a murine bladder infection model. Our results indicate that redundant APRs are weak points of bacterial protein homeostasis and that targeting these may be an attractive antibacterial strategy.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Data-Review
[do] DOI:10.1038/s41467-018-03131-0


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