TY - JOUR AU - Forró, Enikő AU - Fülöp, Ferenc TI - The First Direct Enzymatic Hydrolysis of Alicyclic Beta-amino Esters: A Route to Enantiopure Cis And Trans Beta-amino Acids JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 13 PY - 2007 IS - 22 SP - 6397 EP - 6401 PG - 5 SN - 0947-6539 DO - 10.1002/chem.200700257 UR - https://m2.mtmt.hu/api/publication/1085087 ID - 1085087 AB - The first direct enzymatic method is reported for the synthesis of cis and trans P-amino acid enantiomers through the lipase-catalyzed enantioselective hydrolysis of alicyclic beta-amino esters in organic media. High enantioselectivities (E usually > 100) were observed when the Candida antarctica lipase B catalyzed reactions were performed with H2O (0.5 equivalents) in iPr(2)O at 65 degrees C. The resolved products, obtained in good yields (>= 42%), could be easily separated. LA - English DB - MTMT ER - TY - JOUR AU - Koda, Y AU - Shiotani, K AU - Tóth, István AU - Tsuda, Y AU - Okada, Y AU - Blanchfield, JT TI - Comparison of the in vitro apparent permeability and stability of opioid mimetic compounds with that of the native peptide. JF - BIOORGANIC & MEDICINAL CHEMISTRY LETTERS J2 - BIOORG MED CHEM LETT VL - 17 PY - 2007 IS - 7 SP - 2043 EP - 2046 PG - 4 SN - 0960-894X DO - 10.1016/j.bmcl.2007.01.051 UR - https://m2.mtmt.hu/api/publication/1336023 ID - 1336023 N1 - Megjegyzés-20963332 Megjegyzés-20964109 UR: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847613951&partnerID=40&md5=31a7ec5771305a3ab01573eb3a98f616 AB - Three dimethyl-L-tyrosine (Dmt) based peptide analogues were identified in a previous study as excellent agonists for the mu-opioid receptor showing very low K(i) values and good in vivo antinociceptive activity upon intracerebroventricular administration to mice. This activity decreased markedly when the compounds were delivered subcutaneously or orally. To establish the cause of this decrease of activity the apparent permeability across Caco-2 cell monolayers of each compound and their relative stability to the digestive enzymes present in the cell line has been determined and compared to that of the native peptide endomorphin 2. The compounds' permeabilities clearly correlate with their increasing lipophilicity suggesting that the analogues cross the monolayer via passive diffusion and the results show that the compound with high K(i) value for the mu-receptor (K(i)mu=0.114 nM) exhibited the highest permeability suggesting that this may be the better lead compound despite the lower binding affinity than that of compound 2 or 3. LA - English DB - MTMT ER - TY - JOUR AU - Leitgeb, Balázs TI - Structural investigation of endomorphins by experimental and theoretical methods: Hunting for the bioactive conformation JF - CHEMISTRY & BIODIVERSITY J2 - CHEM BIODIVERS VL - 4 PY - 2007 IS - 12 SP - 2703 EP - 2724 PG - 22 SN - 1612-1872 DO - 10.1002/cbdv.200790221 UR - https://m2.mtmt.hu/api/publication/1915407 ID - 1915407 LA - English DB - MTMT ER - TY - JOUR AU - Fülöp, Ferenc AU - Martinek, Tamás AU - Tóth, Gábor TI - Application of alicyclic beta-amino acids in peptide chemistry JF - CHEMICAL SOCIETY REVIEWS J2 - CHEM SOC REV VL - 35 PY - 2006 IS - 4 SP - 323 EP - 334 PG - 12 SN - 0306-0012 DO - 10.1039/B501173F UR - https://m2.mtmt.hu/api/publication/1012938 ID - 1012938 N1 - Megjegyzés-21956224 Z9: 133 WC: Chemistry, Multidisciplinary Megjegyzés-21957808 Z9: 133 WC: Chemistry, Multidisciplinary CAplus AN 2006:279672; MEDLINE PMID: 16565749 (Journal; General Review; Article; Research Support, Non-U.S. Gov't; Review); AB - The self-organizing beta-peptides have attracted considerable interest in the fields of foldamer chemistry and biochemistry. These compounds exhibit various stable secondary structure motifs that can be exploited to construct biologically active substances and nanostructured tertiary structures. The secondary structures can be controlled via the beta-amino acid sequence, and cyclic beta-amino acid residues play a crucial role in the design. The most important procedures for the preparation of cyclic beta-amino acid monomers and peptides are discussed in this tutorial review. Besides the secondary structure design principles, the methods of folded structure detection are surveyed. LA - English DB - MTMT ER - TY - JOUR AU - Keresztes, Attila AU - Tóth, Géza AU - Fülöp, Ferenc AU - Szűcs, Mária TI - Synthesis, radiolabeling and receptor binding of [H-3][(1S,2R)ACPC(2)]endomorphin-2 JF - PEPTIDES J2 - PEPTIDES VL - 27 PY - 2006 IS - 12 SP - 3315 EP - 3321 PG - 7 SN - 0196-9781 DO - 10.1016/j.peptides.2006.09.004 UR - https://m2.mtmt.hu/api/publication/1078934 ID - 1078934 N1 - Hungarian Acad Sci, Biol Res Ctr, Inst Biochem, H-6701 Szeged, Hungary. Univ Szeged, Inst Pharmaceut Chem, H-6720 Szeged, Hungary. AB - Previously, we have shown that substitution of Pro(2) for cis-2-aminocyclopentanecarboxylic acid, ACPC in endomorphin-2 results in an analogue with greatly augmented proteolytic stability, high mu-opioid receptor affinity and selectivity. We now report the synthesis and biochemical characterization of [H-3][(1S,2R)ACPC(2)]endomorphin-2 with a specific activity of 1.41 TBq/mmol (38.17 Ci/mmol). Specific binding of [3H][(1S,2R)ACPC2]endomorphin-2 was saturable and of high affinity with an equilibrium dissociation constant, K-d = 1.80 +/- 0.21 nM and receptor density, B-max = 345 +/- 27 fmol x mg protein(-1) at 25 degrees C in rat brain membranes. Similar affinity values were obtained in kinetic and displacement assays. Both Na+ and Gpp(NH)p decreased the affinity proving the agonist character of the radioligand. [H-3][(1S,2R)ACPC(2)]endomorphin-2 retained the mu-specificity of the parent peptide. The new radioligand will be a useful tool to map the topographical requirements of mu-opioid peptide binding due to its high affinity, selectivity and enzymatic stability. (c) 2006 Elsevier Inc. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Rónai, András AU - Szemenyei, Erzsébet AU - Kató, Erzsébet AU - Kocsis, László AU - Orosz, György AU - Al-Khrasani, Mahmoud AU - Tóth, Géza TI - Endomorphin synthesis in rat brain from intracerebroventricularly injected [H-3]-Tyr-Pro: A possible biosynthetic route for endomorphins JF - REGULATORY PEPTIDES J2 - REGUL PEPTIDES VL - 134 PY - 2006 IS - 1 SP - 54 EP - 60 PG - 7 SN - 0167-0115 DO - 10.1016/j.regpep.2005.12.004 UR - https://m2.mtmt.hu/api/publication/1626916 ID - 1626916 N1 - Cited By :17 Export Date: 29 May 2022 CODEN: REPPD AB - in spite of concentrated efforts, the biosynthetic route of mu-opioid receptor agonist brain tetrapeptide endomorphins (Tyr-Pro-Trp-Phe-NH2 and Tyr-Pro-Phe-Phe-NH2), discovered in 1997, is still obscure. We report presently that 30 min after intracerebroventricular injection of 20 or 200 mu Ci [H-3]Tyr-Pro (49.9 Ci mmol(-1)) the incorporated radioactivity was found in endomorphin-related tetra- and tripeptides in rat brain extracts. As detected by the combination of HPLC with radiodetection, a peak corresponding to endomorphin-2-OH could be identified in two of four extracts of "20 mu Ci" series. Radioactive peaks in position of Tyr, Tyr-Pro, Tyr-Pro-Phe or Tyr-Pro-Trp appeared regularly in both series and also in the "tetrapeptide cluster" constituted by endomorphins and their free carboxylic forms. In one of the four extracts in the "200 mu Ci" series a robust active peak in the position of endomorphin 2 could be detected. Intracerebroventricularly injected 100 mmol, but not 10 or 1000 nmol cold Tyr-Pro (devoid of opioid activity in vitro), caused a naloxone-reversible prolongation of tail-flick latency in rats, peaking between 15 and 30 min. We suggest that Tyr-Pro may serve as a biosynthetic precursor to endomorphin synthesis. (C) 2006 Elsevier B.V. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Rónai, András AU - Al-Khrasani, Mahmoud AU - Benyhe, Sándor AU - Lengyel, Imre AU - Kocsis, L AU - Orosz, György AU - Tóth, Géza AU - Kató, Erzsébet AU - Tóthfalusi, László TI - Partial and full agonism in endomorphin derivatives: Comparison by null and operational model JF - PEPTIDES J2 - PEPTIDES VL - 27 PY - 2006 IS - 6 SP - 1507 EP - 1513 PG - 7 SN - 0196-9781 DO - 10.1016/j.peptides.2005.12.003 UR - https://m2.mtmt.hu/api/publication/1599754 ID - 1599754 N1 - Cited By :17 Export Date: 29 May 2022 CODEN: PEPTD AB - The partial mu-opioid receptor pool inactivation strategy in isolated mouse vas deferens was used to determine partial agonism of endomorphins and their analogs (endomorphin-1-ol, 2',6'-dimethyltyrosine (Dmt)-endomorphin-1, endomorphin-2-ol and (D-Met 2)-endomorphin-2) using morphine, normorphine, morphiceptin, (D-Ala(2), MePhe(4) Glys-ol)-enkephal\in (DAMGO) and its amide (DAMGA) as reference opioid agonists. Agonist affinities (KA) and efficacies were assessed both by the "null" and the "operational" method. The KA values determined by the two methods correlated significantly with each other and also with the displacing potencies against H-3-naloxone in the receptor binding assay in the presence of Na+. DAMGO and DAMGA were full agonist prototypes, morphine, endomorphin-1, endomorphin-1-ol, Dmt-endomorphin-1, endomorphin-2-ol and (D-Met(2))-endomorphin-2 were found by both methods to be partial agonists whereas the parameters for normorphine, morphiceptin and endomorphin-2 were intermediate. (c) 2005 Elsevier Inc. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Forró, Enikő AU - Fülöp, Ferenc TI - Advanced procedure for the enzymatic ring opening of unsaturated alicyclic beta-lactams JF - TETRAHEDRON-ASYMMETRY J2 - TETRAHEDRON ASYMMETR VL - 15 PY - 2004 IS - 18 SP - 2875 EP - 2880 PG - 6 SN - 0957-4166 DO - 10.1016/j.tetasy.2004.05.029 UR - https://m2.mtmt.hu/api/publication/1013238 ID - 1013238 N1 - Cited By :65 Export Date: 3 June 2023 CODEN: TASYE Correspondence Address: Fülöp, F.; Inst. of Pharmaceutical Chemistry, , Szeged, Hungary; email: fulop@pharma.szote.u-szeged.hu Chemicals/CAS: chloride, 16887-00-6; water, 7732-18-5 Funding details: Hungarian Scientific Research Fund, OTKA, 0115/2001, 181/2002, T 046440, TS 040888 Funding text 1: The authors acknowledge the receipt of OTKA grants TS 040888 and T 046440, FKFP grant 0115/2001 and a Békésy Fellowship for EF (grant no. 181/2002). AB - Enantiopure beta-amino acids 1a-4a and beta-lactams 1b-4b were prepared simultaneously through the lipolase-catalysed enantioselective ring opening of unsaturated racemic beta-lactams (+/-)-1-(+/-)-4. High enantioselectivities (E >200) were observed when the reactions were performed with 1 equiv of water in iPr(2)O at 70degreesC. The resolved (1R,2S)-amino acids (yield greater than or equal to 45%) and (1S,5R)-, (1S,6R)- and (1S,8R)-lactams (yield greater than or equal to47%) could be easily separated. The ring opening of lactam enantiomers 1b-4b with 18% HCl afforded the corresponding beta-amino acid hydrochlorides 1c(.)HCl-4c(.)HCl (ee >95%). (C) 2004 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Tömböly, Csaba AU - E Kövér, Katalin AU - Péter, Antal AU - Tourwe, D AU - Biyashev, D AU - Benyhe, Sándor AU - Borsodi, Anna AU - Al-Khrasani, Mahmoud AU - Rónai, András AU - Tóth, Géza TI - Structure-activity study on the Phe side chain arrangement of endomorphins using conformationally constrained analogues JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 47 PY - 2004 IS - 3 SP - 735 EP - 743 PG - 9 SN - 0022-2623 DO - 10.1021/jm0310028 UR - https://m2.mtmt.hu/api/publication/1154247 ID - 1154247 AB - Endomorphins-1 and -2 were substituted with all the beta-MePhe stereoisomers in their Phe residues to generate a conformationally constrained peptide set. This series of molecules was subjected to biological assays, and for beta-MePhe(4)-endomorphins-2, a conformational analysis was performed. Incorporation of (2S,3S)-beta-MePhe(4) resulted in the most potent analogues of both endomorphins with enhanced enzymatic stability. Their mu opioid affinities were 4-times higher than the parent peptides, they stimulated [S-35]GTPgammaS binding, and they were found to be full agonists. NMR experiments revealed that C-terminal (2S,3S)-beta-MePhe in endomorphin-2 strongly favored the gauche H spatial orientation which implies the presence of the chi(1) = -60degrees rotamer of Phe(4) in the binding conformer of endomorphins. Our results emphasize that the appropriate orientation of the C-terminal aromatic side chain of endomorphins is substantial for binding to the mu opioid receptor. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Géza AU - Keresztes, Attila AU - Tömböly, Csaba AU - Péter, Antal AU - Fülöp, Ferenc AU - Tourwe, D AU - Navratilova, E AU - Varga, Éva AU - Roeske, W R AU - Yamamura, H I AU - Szűcs, Mária AU - Borsodi, Anna TI - New endomorphin analogs with mu-agonist and delta-antagonist properties JF - PURE AND APPLIED CHEMISTRY J2 - PURE APPL CHEM VL - 76 PY - 2004 IS - 5 SP - 951 EP - 957 PG - 7 SN - 0033-4545 DO - 10.1351/pac200476050951 UR - https://m2.mtmt.hu/api/publication/1013246 ID - 1013246 AB - Endomorphins (endomorphin-1, H-Tyr-Pro-Trp-Phe-NH2, endomorphin-2, Tyr-Pro-Phe-Phe-NH2) are potent and selective mu-opioid receptor agonists. In order to improve the affinity and chemical stability of endomorphins, we have designed, synthesized, and characterized novel analogs with unnatural (2', 6'-dimethyltyrosine, Dmt) and/or beta-alicyclic amino acids (ACPC and ACHC). Radioligand binding assay indicated that several of the novel analogs exhibit high affinity for both mu- and delta-opioid receptors in rat- or mouse-brain membrane preparations. The most promising derivatives-such as Dmt-Pro-Trp/Phe-Phe-NH2. Dmt-(1S,2R)-ACPC-Phe-Phe-NH2, and Dmt-(1S,2R)-ACHC-Phe-Phe-NH2)-were characterized in recombinant cell lines expressing human mu- or delta-opioid receptors. Interestingly, while these novel peptides were potent opioid agonists in the functional [S-35]GTPgammaS binding assays in Chinese hamster ovary cells expressing the mu-opioid receptors, some behaved as antagonist or inverse agonist in the human delta-opioid receptor-expressing CHO cells. Since it has previously been demonstrated that the coadministration of delta-antagonists with mu-analgesics attenuates the development of analgesic tolerance, introduction of high-affinity delta-antagonist properties into the mu-agonist endomorphins is expected to lead to potent analgesics that produce limited tolerance. LA - English DB - MTMT ER - TY - JOUR AU - Wollemann, Mária AU - Benyhe, Sándor TI - Non-opioid actions of opioid peptides JF - LIFE SCIENCES J2 - LIFE SCI VL - 75 PY - 2004 SP - 257 EP - 270 PG - 14 SN - 0024-3205 DO - 10.1016/j.lfs.2003.12.005 UR - https://m2.mtmt.hu/api/publication/1913444 ID - 1913444 N1 - Cited By :67 Export Date: 22 June 2022 CODEN: LIFSA LA - English DB - MTMT ER - TY - JOUR AU - Forró, Enikő AU - Fülöp, Ferenc TI - Lipase-catalyzed enantioselective ring opening of unactivated alicyclic-fused beta-lactams in an organic solvent JF - ORGANIC LETTERS J2 - ORG LETT VL - 5 PY - 2003 SP - 1209 EP - 1212 PG - 4 SN - 1523-7060 DO - 10.1021/ol034096o UR - https://m2.mtmt.hu/api/publication/1013530 ID - 1013530 N1 - Megjegyzés-21956242 Z9: 55 WC: Chemistry, Organic Megjegyzés-26797570 N1 CAPLUS AN 2003:213291(Journal) AB - A highly efficient and very simple method was developed for the synthesis of enantiopure beta-amino acids (e.g. cispentacin) and beta-lactams through the enzyme-catalyzed enantioselective ring opening of unactivated alicyclic, beta-lactams in organic media. High enantioselectivity (E > 200) was observed when the Lipolase flipase B from Candida antarctica)-catalyzed reactions were performed with H2O (1 equiv) in dilsopropyl ether at 60 degreesC. The resolved products, obtained in good chemical yield (36-47%), could be easily separated. LA - English DB - MTMT ER - TY - JOUR AU - Leitgeb, Balázs AU - Ötvös, Ferenc AU - Tóth, Géza TI - Conformational analysis of endomorphin-2 by molecular dynamics methods JF - BIOPOLYMERS J2 - BIOPOLYMERS VL - 68 PY - 2003 SP - 497 EP - 511 PG - 15 SN - 0006-3525 DO - 10.1002/bip.10333 UR - https://m2.mtmt.hu/api/publication/1912835 ID - 1912835 LA - English DB - MTMT ER - TY - JOUR AU - Ötvös, Ferenc AU - Körtvélyesi, Tamás AU - Tóth, Géza TI - Structure-activity relationships of endomorphin-1, endomorphin-2 and morphiceptin by molecular dynamics methods JF - JOURNAL OF MOLECULAR STRUCTURE: THEOCHEM J2 - J MOL STRUC-THEOCHEM VL - 666-667 PY - 2003 SP - 345 EP - 353 PG - 9 SN - 0166-1280 DO - 10.1016/j.theochem.2003.08.044 UR - https://m2.mtmt.hu/api/publication/1913540 ID - 1913540 LA - English DB - MTMT ER - TY - JOUR AU - Fábián, Gabriella AU - Bozó, Bea AU - Szikszay, M AU - Horváth, Gyöngyi AU - Coscia, CJ AU - Szűcs, Mária TI - Chronic morphine-induced changes in mu-opioid receptors and G proteins of different subcellular loci in rat brain JF - JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS J2 - J PHARMACOL EXP THER VL - 302 PY - 2002 IS - 2 SP - 774 EP - 780 PG - 7 SN - 0022-3565 DO - 10.1124/jpet.102.036152 UR - https://m2.mtmt.hu/api/publication/1822624 ID - 1822624 N1 - WoS:hiba:000176899200047 2019-03-03 09:45 cikkazonosító nem egyezik LA - English DB - MTMT ER - TY - JOUR AU - Tömböly, Csaba AU - Péter, Antal AU - Tóth, Géza TI - In vitro quantitative study of the degradation of endomorphins JF - PEPTIDES J2 - PEPTIDES VL - 23 PY - 2002 IS - 9 SP - 1573 EP - 1580 PG - 8 SN - 0196-9781 DO - 10.1016/S0196-9781(02)00100-6 UR - https://m2.mtmt.hu/api/publication/1322897 ID - 1322897 N1 - WoS:hiba:000178339300006 2019-03-02 02:14 cikkazonosító nem egyezik LA - English DB - MTMT ER - TY - JOUR AU - Fülöp, Ferenc TI - The chemistry of 2-aminocycloalkanecarboxylic acids JF - CHEMICAL REVIEWS J2 - CHEM REV VL - 101 PY - 2001 IS - 7 SP - 2181 EP - 2204 PG - 24 SN - 0009-2665 DO - 10.1021/cr000456z UR - https://m2.mtmt.hu/api/publication/1013895 ID - 1013895 N1 - Cited By :361 Export Date: 3 June 2023 CODEN: CHREA Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chem., POB 121, H-6701 Szeged, Hungary; email: fulop@pharma.szote.u-szeged.hu Chemicals/CAS: Acids, Carbocyclic; Amino Acids, Cyclic; Analgesics, Opioid; Antifungal Agents; Antineoplastic Agents LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Gyöngyi AU - Szikszay, M AU - Tömböly, Csaba AU - Benedek, György TI - Antinociceptive effects of intrathecal endomorphin-1 and -2 in rats. JF - LIFE SCIENCES J2 - LIFE SCI VL - 65 PY - 1999 IS - 24 SP - 2635 EP - 2641 PG - 7 SN - 0024-3205 DO - 10.1016/S0024-3205(99)00532-9 UR - https://m2.mtmt.hu/api/publication/1340987 ID - 1340987 AB - Endomorphin-1 and endomorphin-2 were recently postulated to be endogenous mu-opioid receptor agonists. We have investigated the antinociceptive and antihyperalgesic effects of intrathecally administered endomorphins in cumulative doses (0.1-100 microg) on acute and inflammatory pain sensations in awake rats. In the tail-flick test, both peptides caused a dose-dependent short-lasting antinociception, except at the highest dose, which caused motor impairment also. The dose-response curves revealed the development of acute tolerance (tachyphylaxis) to endomorphin. Similarly in the carrageenan-injected paw, the endomorphins (10 microg) exerted transient antinociceptive effects. These are the first data to demonstrate decreased responsivity in models of both acute and inflammatory pain after intrathecal administration of endomorphin-1 and -2 in awake rats. LA - English DB - MTMT ER - TY - JOUR AU - Péter, Antal AU - Tóth, Géza AU - Tömböly, Csaba AU - Laus, G AU - Tourwe, D TI - Liquid chromatographic study of the enzymatic degradation of endomorphins, with identification by electrospray ionization mass spectrometry JF - JOURNAL OF CHROMATOGRAPHY A J2 - J CHROMATOGR A VL - 846 PY - 1999 IS - 1-2 SP - 39 EP - 48 PG - 10 SN - 0021-9673 DO - 10.1016/S0021-9673(99)00146-6 UR - https://m2.mtmt.hu/api/publication/1322914 ID - 1322914 LA - English DB - MTMT ER - TY - JOUR AU - PRZEWLOCKA, B AU - MIKA, J AU - LABUZ, D AU - Tóth, Géza AU - PRZEWLOCKI, R TI - Spinal analgesic action of endomorphins in acute, inflammatory and neuropathic pain in rats JF - EUROPEAN JOURNAL OF PHARMACOLOGY J2 - EUR J PHARMACOL VL - 367 PY - 1999 SP - 189 EP - 196 PG - 8 SN - 0014-2999 DO - 10.1016/S0014-2999(98)00956-X UR - https://m2.mtmt.hu/api/publication/1910774 ID - 1910774 LA - English DB - MTMT ER - TY - JOUR AU - E Kövér, Katalin AU - Uhrin, D AU - Hruby, VJ TI - Gradient- and sensitivity-enhanced TOCSY experiments JF - JOURNAL OF MAGNETIC RESONANCE J2 - J MAGN RESON VL - 130 PY - 1998 IS - 2 SP - 162 EP - 168 PG - 7 SN - 1090-7807 DO - 10.1006/jmre.1997.1309 UR - https://m2.mtmt.hu/api/publication/1154216 ID - 1154216 AB - A pulsed held gradient version of the sensitivity-enhanced 2D TOCSY experiment is proposed which yields high-quality spectra with improved sensitivity and a minimum of two scans per t(1) increment, For rapid acquisition of 1D TOCSY spectra, the 1D DPFGSE-TOCSY experiment was modified to include phase-encoded multiple-selective excitation followed by a simple spectral editing. Combination of these two building blocks is used in a sensitivity-enhanced 2D analog of the 3D TOCSY-TOCSY experiment which provides an efficient tool for resolving severely overlapped signals of oligomers in short experimental time. (C) 1998 Academic Press. LA - English DB - MTMT ER - TY - JOUR AU - Spetea, Mariana AU - Monory, Krisztina AU - Tömböly, Csaba AU - Tóth, Géza AU - TZAVARA, E AU - Benyhe, Sándor AU - HANOUNE, J AU - Borsodi, Anna TI - In Vitro Binding and Signaling Profile of the Novel Mu Opioid Receptor Agonist Endomorphin 2 in Rat Brain Membranes JF - BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS J2 - BIOCHEM BIOPH RES CO VL - 250 PY - 1998 SP - 720 EP - 725 PG - 6 SN - 0006-291X DO - 10.1006/bbrc.1998.9395 UR - https://m2.mtmt.hu/api/publication/1910511 ID - 1910511 N1 - Megjegyzés-21981571 Chemicals/CAS: Analgesics, Opioid; endomorphin 2; Oligopeptides; Receptors, Opioid, mu Tradenames: u 69593, du pont new england nuclear, United States Manufacturers: du pont new england nuclear, United States; sigma, United States LA - English DB - MTMT ER - TY - JOUR AU - Bozó, Bea AU - Fülöp, Ferenc AU - Tóth, Gábor AU - Tóth, Géza AU - Szűcs, Mária TI - Synthesis and opioid binding activity of dermorphin analogues containing cyclic beta-amino acids. JF - NEUROPEPTIDES J2 - NEUROPEPTIDES VL - 31 PY - 1997 IS - 4 SP - 367 EP - 372 PG - 6 SN - 0143-4179 DO - 10.1016/S0143-4179(97)90073-1 UR - https://m2.mtmt.hu/api/publication/1907306 ID - 1907306 AB - In the present work, eight conformationally constrained analogues of the mu specific opioid peptide dermorphin were synthesized by replacing D-Ala(2) with stereoisomers of beta-amino-cycloalkane or cycloalkene carboxylic acids. The resulting peptides were tested for their potency to mu and delta opioid binding sites of rat brain membranes labelled with [H-3]Tyr(1)-D-Ala(2)-MePhe(4)-Gly-ol, [H-3]DAMGO and [H-3]Ile(5,6)deltorphin, respectively. All of the new derivatives displayed highly attenuated binding to both receptor types, albeit the decrease in their potency seemed to be less in the case of 6 binding. Trans position of the beta-amino groups resulted in higher binding affinities than that of the corresponding cis isomers, the latter being more flexible than the former. It is concluded that conformational constraints caused either by a rigid ring structure or cis isomers instead of D-Ala(2) in dermorphin-derived peptides are unfavourable for binding activity to either opioid receptors. We propose that interaction of the larger heptapeptide derivatives of dermorphins with the mu receptor is distinct from that of the tetrapeptide morphiceptin. LA - English DB - MTMT ER - TY - JOUR AU - Péter, Antal AU - Fülöp, Ferenc TI - HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHIC METHOD FOR THE SEPARATION OF ISOMERS OF CIS-2-AMINO-CYCLOPENTANE-1-CARBOXYLIC AND TRANS-2-AMINO-CYCLOPENTANE-1-CARBOXYLIC ACID JF - JOURNAL OF CHROMATOGRAPHY A J2 - J CHROMATOGR A VL - 715 PY - 1995 SP - 219 EP - 226 PG - 8 SN - 0021-9673 DO - 10.1016/0021-9673(95)00615-T UR - https://m2.mtmt.hu/api/publication/1015649 ID - 1015649 LA - English DB - MTMT ER -