TY - JOUR AU - Szaniszló, Szebasztián AU - Csámpai, Antal AU - Horváth, Dániel AU - Tomecz, Richárd AU - Farkas, Viktor AU - Perczel, András TI - Unveiling the Oxazolidine Character of Pseudoproline Derivatives by Automated Flow Peptide Chemistry JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 25 PY - 2024 IS - 8 SP - 4150 SN - 1661-6596 DO - 10.3390/ijms25084150 UR - https://m2.mtmt.hu/api/publication/34781847 ID - 34781847 AB - Pseudoproline derivatives such as Thr(ΨPro)-OH are commonly used in peptide synthesis to reduce the likelihood of peptide aggregation and to prevent aspartimide (Asi) formation during the synthesis process. In this study, we investigate notable by-products such as aspartimide formation and an imine derivative of the Thr(ΨPro) moiety observed in flow peptide chemistry synthesis. To gain insight into the formation of these unexpected by-products, we design a series of experiments. Furthermore, we demonstrate the oxazolidine character of the pseudoproline moiety and provide plausible mechanisms for the two-way ring opening of oxazolidine leading to these by-products. In addition, we present evidence that Asi formation appears to be catalyzed by the presence of the pseudoproline moiety. These observed side reactions are attributed to elevated temperature and pressure; therefore, caution is advised when using ΨPro derivatives under such harsh conditions. In addition, we propose a solution whereby thermodynamically controlled Asi formation can be kinetically prevented. LA - English DB - MTMT ER - TY - JOUR AU - Tarchoun, Karima AU - Soltész, Dóra AU - Farkas, Viktor AU - Lee, Ho-Jin AU - Szabó, Ildikó AU - Bánóczi, Zoltán TI - Influence of Aza-Glycine Substitution on the Internalization of Penetratin JF - PHARMACEUTICS J2 - PHARMACEUTICS VL - 16 PY - 2024 IS - 4 SP - 477 SN - 1999-4923 DO - 10.3390/pharmaceutics16040477 UR - https://m2.mtmt.hu/api/publication/34765015 ID - 34765015 AB - The cell-penetrating peptide (CPP) penetratin has gained much attention over many years due to its potential role as a transporter for a broad range of cargo into cells. The modification of penetratin has been extensively investigated too. Aza-peptides are peptide analogs in which one or more of the amino residues are replaced by a semicarbazide. This substitution results in conformational restrictions and modifications in hydrogen bonding properties, which affect the structure and may lead to enhanced activity and selectivity of the modified peptide. In this work, the Trp residues of penetratin were substituted by aza-glycine or glycine residues to examine the effect of these modifications on the cellular uptake and the internalization mechanism. The substitution of Trp48 or Trp48,56 dramatically reduced the internalization, showing the importance of Trp48 in cellular uptake. Interestingly, while aza-glycine in the position of Trp56 increased the cellular uptake, Gly reduced it. The two Trp-modified derivatives showed altered internalization pathways, too. Based on our knowledge, this is the first study about the effect of aza-amino acid substitution on the cell entry of CPPs. Our results suggest that aza-amino acid insertion is a useful modification to change the internalization of a CPP. LA - English DB - MTMT ER - TY - JOUR AU - Ferentzi, Kristóf AU - Nagy-Fazekas, Dóra AU - Farkas, Viktor AU - Perczel, András TI - Synthesis of small protein domains by automated flow chemistry JF - REACTION CHEMISTRY & ENGINEERING J2 - REACT CHEM ENG VL - 9 PY - 2023 IS - 1 SP - 58 EP - 69 PG - 12 SN - 2058-9883 DO - 10.1039/D3RE00324H UR - https://m2.mtmt.hu/api/publication/34398184 ID - 34398184 N1 - Hevesy György PhD School of Chemistry, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány. 1/A, Budapest, H-1117, Hungary Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány. 1/A, Budapest, H-1117, Hungary HUN-REN-ELTE Protein Modeling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány. 1/A, Budapest, H-1117, Hungary Export Date: 2 April 2024 Correspondence Address: Perczel, A.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány. 1/A, Hungary; email: perczel.andras@ttk.elte.hu AB - The most fundamental topological units of proteins are their autonomously folded domains. The rapid and reliable chemical synthesis of domains in the range of 5-10 kDa in size, remains a... LA - English DB - MTMT ER - TY - JOUR AU - Szaniszló, Szebasztián AU - Ferentzi, Kristóf AU - Perczel, András AU - Farkas, Viktor TI - Improved Acylation of Pseudoproline: Masked Threonine in Flow Peptide Chemistry JF - ORGANIC PROCESS RESEARCH & DEVELOPMENT J2 - ORG PROCESS RES DEV VL - 27 PY - 2023 IS - 6 SP - 1053 EP - 1060 PG - 8 SN - 1083-6160 DO - 10.1021/acs.oprd.3c00029 UR - https://m2.mtmt.hu/api/publication/34014650 ID - 34014650 N1 - Export Date: 2 October 2023 CODEN: OPRDF Correspondence Address: Perczel, A.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány. 1/A, Hungary; email: perczel.andras@ttk.elte.hu Correspondence Address: Farkas, V.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány. 1/A, Hungary; email: farkas.viktor@ttk.elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Bencs, Fruzsina AU - Farkas, Viktor AU - Perczel, András TI - Early stage amyloid formation probed: what makes cross-beta spine stable JF - JOURNAL OF PEPTIDE SCIENCE J2 - J PEPT SCI VL - 28 PY - 2022 PG - 1 SN - 1075-2617 UR - https://m2.mtmt.hu/api/publication/34034560 ID - 34034560 N1 - Supplement: 3 LA - English DB - MTMT ER - TY - JOUR AU - Keresztes, László AU - Szögi, Evelin AU - Varga, Bálint AU - Farkas, Viktor AU - Perczel, András AU - Grolmusz, Vince TI - Succinct Amyloid and Nonamyloid Patterns in Hexapeptides JF - ACS OMEGA J2 - ACS OMEGA VL - 7 PY - 2022 IS - 40 SP - 35532 EP - 35537 PG - 6 SN - 2470-1343 DO - 10.1021/acsomega.2c02513 UR - https://m2.mtmt.hu/api/publication/33155481 ID - 33155481 N1 - PIT Bioinformatics Group, Eötvös University, Budapest, H-1117, Hungary Uratim Ltd., Budapest, H-1118, Hungary MTA-ELTE Protein Modeling Research Group, Budapest, H-1117, Hungary Laboratory of Structural Chemistry and Biology, Eötvös University, Budapest, H-1117, Hungary Export Date: 8 May 2023 Correspondence Address: Grolmusz, V.; PIT Bioinformatics Group, Hungary; email: grolmusz@pitgroup.org LA - English DB - MTMT ER - TY - GEN AU - Laszlo, Keresztes AU - Evelin, Szogi AU - Balint, Varga AU - Farkas, Viktor AU - Perczel, András AU - Grolmusz, Vince TI - Succinct Amyloid and Non-Amyloid Patterns in Hexapeptides PY - 2022 UR - https://m2.mtmt.hu/api/publication/32725488 ID - 32725488 AB - Hexapeptides are widely applied as a model system for studying amyloid-forming properties of polypeptides, including proteins. Recently, large experimental databases have become publicly available with amyloidogenic labels. Using these datasets for training and testing purposes, one may build artificial intelligence (AI)-based classifiers for predicting the amyloid state of peptides. In our previous work (Biomolecules, 11(4) 500, (2021)) we described the Support Vector Machine (SVM)-based Budapest Amyloid Predictor (\url{this https URL}). Here we apply the Budapest Amyloid Predictor for discovering numerous amyloidogenic and non-amyloidogenic hexapeptide patterns with accuracy between 80\% and 84\%, as surprising and succinct novel rules for further understanding the amyloid state of peptides. For example, we have shown that for any independently mutated residue (position marked by ``x''), the patterns CxFLWx, FxFLFx, or xxIVIV are predicted to be amyloidogenic, while those of PxDxxx, xxKxEx, and xxPQxx non-amyloidogenic at all. We note that each amyloidogenic pattern with two x's (e.g.,CxFLWx) describes succinctly 202=400 hexapeptides, while the non-amyloidogenic patterns comprising four point mutations (e.g.,PxDxxx) gives 204=160,000 hexapeptides in total. To our knowledge, no similar applications of artificial intelligence tools or succinct amyloid patterns were described before the present work. LA - English DB - MTMT ER - TY - JOUR AU - Szigyarto, Imola AU - El, Battioui Kamal AU - Farkas, Viktor AU - Wacha, András Ferenc AU - Mihaly, Judith AU - Schlosser, Gitta (Vácziné) AU - Juhasz, Tunde AU - Románszki, Loránd AU - Varga, Zoltan AU - Mandity, Istvan AU - Beke-Somfai, Tamas TI - Self-assembled and membrane active beta[sup]3 [/sup]-peptides: from design to application JF - JOURNAL OF PEPTIDE SCIENCE J2 - J PEPT SCI VL - 28 PY - 2022 IS - Supplement3 PG - 2 SN - 1075-2617 UR - https://m2.mtmt.hu/api/publication/34034758 ID - 34034758 N1 - Funding text: This work was funded by Momentum programme (LP2016-2 (T. B-S.)) of the Hungarian Academy of Sciences, National Competitiveness and Excellence Program (NVKP_16-1-2016-0007) and BIONANO_GINOP-2.3.2-15-2016-00017 grants. Published AUG 2022 LA - English DB - MTMT ER - TY - JOUR AU - Farkas, Viktor AU - Ferentzi, Kristóf AU - Horváti, Kata AU - Perczel, András TI - Cost-Effective Flow Peptide Synthesis: Metamorphosis of HPLC JF - ORGANIC PROCESS RESEARCH & DEVELOPMENT J2 - ORG PROCESS RES DEV VL - 25 PY - 2021 IS - 2 SP - 182 EP - 191 PG - 10 SN - 1083-6160 DO - 10.1021/acs.oprd.0c00178 UR - https://m2.mtmt.hu/api/publication/31816042 ID - 31816042 N1 - Funding Agency and Grant Number: Hungarian Ministry for Innovation and Technology; Hungarian Ministry of Human Capacities [1783-3/2018/FEKUTSTRAT]; European UnionEuropean Commission; State of Hungary - European Regional Development Fund [VEKOP-2.3.3-15-2017-00020, VEKOP-2.3.2-16-201700014]; National Research Development and Innovation Fund of Hungary [2018-1.2.1-NKP-2018-00005]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Premium Postdoctoral Research Program of the Hungarian Academy of Sciences Funding text: The authors gratefully acknowledge Janos Szolomajer for the synthesis on CEM Liberty Blue Automated Microwave Peptide Synthesizer. This work was completed in the ELTE Thematic Excellence Programme (Szint+) supported by the Hungarian Ministry for Innovation and Technology. ELTE Institutional Excellence Program (1783-3/2018/FEKUTSTRAT) supported by the Hungarian Ministry of Human Capacities and grants from the European Union and the State of Hungary cofinanced by the European Regional Development Fund (VEKOP-2.3.3-15-2017-00020, VEKOP-2.3.2-16-201700014). Project no 2018-1.2.1-NKP-2018-00005 was implemented with the support provided from the National Research Development and Innovation Fund of Hungary V.F. was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences. K.H. was supported by the Premium Postdoctoral Research Program of the Hungarian Academy of Sciences. LA - English DB - MTMT ER - TY - JOUR AU - Goldschmidt Gőz, Viktória AU - Duong, Kim Hoang Yen AU - Horváth, Dániel AU - Ferentzi, Kristóf AU - Farkas, Viktor AU - Perczel, András TI - Application of Sugar Amino Acids: Flow chemistry used for α/β‐chimera synthesis JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2021 PY - 2021 IS - 44 SP - 6071 EP - 6083 PG - 13 SN - 1434-193X DO - 10.1002/ejoc.202100943 UR - https://m2.mtmt.hu/api/publication/32467225 ID - 32467225 N1 - MTA-ELTE Protein Modeling Research Group, Eötvös Loránd Research Network (ELKH) ELTE Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest, 1117, Hungary Laboratory of Structural Chemistry and Biology, Institute of Chemistry, ELTE Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest, 1117, Hungary Hevesy György PhD School of Chemistry, Institute of Chemistry, ELTE Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest, 1117, Hungary Export Date: 11 July 2022 CODEN: EJOCF Correspondence Address: Perczel, A.; MTA-ELTE Protein Modeling Research Group, Pázmány P. stny. 1/A, Hungary; email: perczel.andras@ttk.elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Keresztes, László AU - Szögi, Evelin AU - Varga, Bálint AU - Farkas, Viktor AU - Perczel, András AU - Grolmusz, Vince TI - The Budapest Amyloid Predictor and Its Applications JF - BIOMOLECULES J2 - BIOMOLECULES VL - 11 PY - 2021 IS - 4 SN - 2218-273X DO - 10.3390/biom11040500 UR - https://m2.mtmt.hu/api/publication/31941873 ID - 31941873 N1 - Funding Agency and Grant Number: European UnionEuropean Commission; State of Hungary; European Regional Development FundEuropean Commission; European Social FundEuropean Social Fund (ESF); ELTE Thematic Excellence Programme (Szint+) - Hungarian Ministry for Innovation and Technology; [VEKOP-2.3.2-16-2017-00014]; [NKFI-127909]; [EFOP-3.6.3-VEKOP-16-2017-00002] Funding text: B.V. and V.G. were partially supported by the VEKOP-2.3.2-16-2017-00014 program, supported by the European Union and the State of Hungary, co-financed by the European Regional Development Fund, L.K., E.S. and V.G. by the NKFI-127909 L.K., E.S. and V.G. were supported in part by the EFOP-3.6.3-VEKOP-16-2017-00002 grant, supported by the European Union, co-financed by the European Social Fund. L.K., E.S., A.P., V.F. and V.G. were partially supported by the ELTE Thematic Excellence Programme (Szint+) supported by the Hungarian Ministry for Innovation and Technology. All authors have read and agreed to the published version of the manuscript. LA - English DB - MTMT ER - TY - JOUR AU - Santa, A. AU - Keresztes, M. AU - Nagy-Kanta, E. AU - Hegedus, J. AU - Farkas, Viktor AU - Batta, Gyula AU - Gáspári, Zoltán AU - Peterfia, B. TI - Characterization of the interaction between Shank-PDZ and GKAP-GH1 domains JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 11 PY - 2021 IS - Suppl. 1 SP - 200 EP - 201 PG - 2 SN - 2211-5463 UR - https://m2.mtmt.hu/api/publication/32152017 ID - 32152017 LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Dániel AU - Taricska, Nóra AU - Keszei, Ernő AU - Stráner, Pál AU - Farkas, Viktor AU - Tóth, Gábor AU - Perczel, András TI - Compactness of Protein Folds Alters Disulfide-Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 21 PY - 2020 IS - 5 SP - 681 EP - 695 PG - 16 SN - 1439-4227 DO - 10.1002/cbic.201900470 UR - https://m2.mtmt.hu/api/publication/30941240 ID - 30941240 N1 - Funding Agency and Grant Number: European UnionEuropean Union (EU) [653706]; State of Hungary; European Regional Development FundEuropean Union (EU) [VEKOP-2.3.3-15-2016-00009, VEKOP-2.3.2-16-2017-00014]; NKFIH of the Hungarian Academy of Sciences [K116305 OTKA]; Jnos Bolyai Research Scholarship of the Hungarian Academy of Sciences Funding text: We thank Dra K. Menyhrd and Istvn Pintr for scientific discussions, Frank Lchr for CPMG measurements, and Zsanett Szegvri and Andrs Koltai for their enthusiastic assistance. NMR spectrometer measurement time (700 MHz Bruker) was courtesy of a MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. The Centre for Biomolecular Magnetic Resonance at the University Frankfurt (BMRZ) provided access for the CPMG measurements in project iNext, a Horizon 2020 programme of the European Union (H2020 grant no. 653706). This research project was supported by the State of Hungary and cofinanced by the European Regional Development Fund (VEKOP-2.3.3-15-2016-00009 and VEKOP-2.3.2-16-2017-00014) and the K116305 OTKA grant of the NKFIH of the Hungarian Academy of Sciences. This paper was supported by the Jnos Bolyai Research Scholarship of the Hungarian Academy of Sciences (to V.F.) Laboratory of Structural Chemistry and Biology and, MTA-ELTE Protein Modeling Research Group at the Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, Budapest, 1518, Hungary Chemical Kinetics Laboratory, Institute of Chemistry, Eötvös Loránd University, 112, P. O. Box 32, Budapest, 1518, Hungary Department of Medical Chemistry, Faculty of General Medicine, University of Szeged, Szeged Dóm tér 8, Szeged, H-6720, Hungary Cited By :1 Export Date: 15 August 2021 CODEN: CBCHF Correspondence Address: Perczel, A.; Laboratory of Structural Chemistry and Biology and, 112, P. O. Box 32, Hungary; email: perczel@chem.elte.hu Funding Agency and Grant Number: European UnionEuropean Commission [653706]; State of Hungary; European Regional Development FundEuropean Commission [VEKOP-2.3.3-15-2016-00009, VEKOP-2.3.2-16-2017-00014]; NKFIH of the Hungarian Academy of SciencesNational Research, Development & Innovation Office (NRDIO) - Hungary [K116305 OTKA]; Jnos Bolyai Research Scholarship of the Hungarian Academy of Sciences Funding text: We thank Dra K. Menyhrd and Istvn Pintr for scientific discussions, Frank Lchr for CPMG measurements, and Zsanett Szegvri and Andrs Koltai for their enthusiastic assistance. NMR spectrometer measurement time (700 MHz Bruker) was courtesy of a MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. The Centre for Biomolecular Magnetic Resonance at the University Frankfurt (BMRZ) provided access for the CPMG measurements in project iNext, a Horizon 2020 programme of the European Union (H2020 grant no. 653706). This research project was supported by the State of Hungary and cofinanced by the European Regional Development Fund (VEKOP-2.3.3-15-2016-00009 and VEKOP-2.3.2-16-2017-00014) and the K116305 OTKA grant of the NKFIH of the Hungarian Academy of Sciences. This paper was supported by the Jnos Bolyai Research Scholarship of the Hungarian Academy of Sciences (to V.F.) AB - A new approach to monitor disulfide-bond reduction in the vicinity of aromatic cluster(s) has been derived by using the near-UV range (lambda=266-293 nm) of electronic circular dichroism (ECD) spectra. By combining the results from NMR and ECD spectroscopy, the 3D fold characteristics and associated reduction rate constants (k) of E19_SS, which is a highly thermostable, disulfide-bond reinforced 39-amino acid long exenatide mimetic, and its N-terminally truncated derivatives have been determined under different experimental conditions. Single disulfide bond reduction of the E19_SS model (with an 18-fold excess of tris(2-carboxyethyl)phosphine, pH 7, 37 degrees C) takes hours, which is 20-30 times longer than that expected, and thus, would not reach completion by applying commonly used reduction protocols. It is found that structural, steric, and electrostatic factors influence the reduction rate, resulting in orders of magnitude differences in reduction half-lives (900>t(1/2)>1 min) even for structurally similar, well-folded derivatives of a small model protein. LA - English DB - MTMT ER - TY - JOUR AU - Farkas, Viktor AU - Nagy, Adrienn AU - Karancsiné Menyhárd, Dóra AU - Perczel, András TI - Assignment of Vibrational Circular Dichroism Cross-Referenced Electronic Circular Dichroism Spectra of Flexible Foldamer Building Blocks: Towards Assigning Pure Chiroptical Properties of Foldamers JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 25 PY - 2019 IS - 65 SP - 14890 EP - 14900 PG - 11 SN - 0947-6539 DO - 10.1002/chem.201903023 UR - https://m2.mtmt.hu/api/publication/30937506 ID - 30937506 N1 - MTA-ELTE Protein Modelling Research Group, Institute of Chemistry, Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest, 1117, Hungary Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány P. stny. 1/A, Budapest, 1117, Hungary Export Date: 5 April 2024 CODEN: CEUJE Correspondence Address: Farkas, V.; MTA-ELTE Protein Modelling Research Group, Pázmány P. stny. 1/A, Hungary; email: farkasv@caesar.elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Goldschmidt Gőz, Viktória AU - Nagy, Adrienn AU - Farkas, Viktor AU - Keszei, Ernő AU - Perczel, András TI - Unwanted hydrolysis or alpha/beta-peptide bond formation: how long should the rate-limiting coupling step take? JF - RSC ADVANCES J2 - RSC ADV VL - 9 PY - 2019 IS - 53 SP - 30720 EP - 30728 PG - 9 SN - 2046-2069 DO - 10.1039/c9ra06124j UR - https://m2.mtmt.hu/api/publication/30859729 ID - 30859729 N1 - Funding Agency and Grant Number: European UnionEuropean Union (EU); State of Hungary; European Regional Development FundEuropean Union (EU) [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Hungarian Academy of SciencesHungarian Academy of Sciences Funding text: The authors wish to thank Daniel Horvath for helping 700 MHz NMR measurements and Tamas Martinek for Fmoc-ACPC-OH, Fmoc-ACHC-OH and linear beta-amino acids. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. Funding Agency and Grant Number: European UnionEuropean Commission; State of Hungary; European Regional Development FundEuropean Commission [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Hungarian Academy of SciencesHungarian Academy of Sciences Funding text: The authors wish to thank Daniel Horvath for helping 700 MHz NMR measurements and Tamas Martinek for Fmoc-ACPC-OH, Fmoc-ACHC-OH and linear beta-amino acids. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. AB - Nowadays, in Solid Phase Peptide Synthesis (SPPS), being either manual, automated, continuous flow or microwave-assisted, the reaction with various coupling reagents takes place via in situ active ester formation. In this study, the formation and stability of these key active esters were investigated with time-resolved H-1 NMR by using the common PyBOP/DIEA and HOBt/DIC coupling reagents for both alpha- and beta-amino acids. Parallel to the amide bond formation, the hydrolysis of the alpha/beta-active esters, a side reaction that is a considerable efficacy limiting factor, was studied. Based on the chemical nature/constitution of the active esters, three amino acid categories were determined: (i) the rapidly hydrolyzing ones (t < 6 h) with smaller (Ala) or even longer side chains (Arg) holding a large protecting group; (ii) branched amino acids (Ile, Thr) with slowly hydrolyzing (6 < t < 24 h) propensities, and (iii) non-hydrolyzing ones, such as the hard-to-couple beta-amino acids or beta-sugar amino acid derivatives, stable for longer times (t > 24 h) in solution. The current insight into the kinetics of this key hydrolysis side reaction serves as a guide to optimize the coupling conditions of alpha- and beta-amino acids, thereby saving time and minimizing the amounts of reagents and amino acids to be used - all key factors of more environmentally friendly chemistry. LA - English DB - MTMT ER - TY - JOUR AU - Horváti, Kata AU - Pályi, Bernadett AU - Henczkó, Judit AU - Balka, Gyula AU - Szabó, Eleonóra AU - Farkas, Viktor AU - Biri-Kovács, Beáta AU - Szeder, Bálint AU - Fodor, Kinga TI - A Convenient Synthetic Method to Improve Immunogenicity of Mycobacterium tuberculosis Related T-Cell Epitope Peptides JF - VACCINES (BASEL) J2 - VACCINES-BASEL VL - 7 PY - 2019 IS - 3 PG - 15 SN - 2076-393X DO - 10.3390/vaccines7030101 UR - https://m2.mtmt.hu/api/publication/30777753 ID - 30777753 N1 - MTA-ELTE Research Group of Peptide Chemistry, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest, 1117, Hungary Institute of Chemistry, Eötvös Loránd University, Budapest, 1117, Hungary National Biosafety Laboratory, National Public Health Center, Budapest, 1097, Hungary Department of Pathology, University of Veterinary Medicine, Budapest, 1078, Hungary Laboratory of Bacteriology, Korányi National Institute for Tuberculosis and Respiratory Medicine, Budapest, 1122, Hungary MTA-ELTE Protein Modelling Research Group, Eötvös Loránd University, Hungarian Academy of Sciences, Budapest, 1117, Hungary Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, 1117, Hungary Department of Laboratory Animal and Animal Protection, University of Veterinary Medicine, Budapest, 1078, Hungary Cited By :7 Export Date: 2 April 2024 Correspondence Address: Horváti, K.; MTA-ELTE Research Group of Peptide Chemistry, Hungary; email: khorvati@elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Adrienn AU - Goldschmidt Gőz, Viktória AU - Pintér, István AU - Farkas, Viktor AU - Perczel, András TI - α/β-Chimera peptide synthesis with cyclic β-sugar amino acids: the efficient coupling protocol JF - AMINO ACIDS J2 - AMINO ACIDS VL - 51 PY - 2019 IS - 4 SP - 669 EP - 678 PG - 10 SN - 0939-4451 DO - 10.1007/s00726-019-02702-9 UR - https://m2.mtmt.hu/api/publication/30435771 ID - 30435771 N1 - Funding Agency and Grant Number: Eotvos Lorand University (ELTE); European Union; State of Hungary; European Regional Development Fund [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences Funding text: Open access funding provided by Eotvos Lorand University (ELTE). The authors wish to thank Dora K. Menyhard and Erno Keszei for consulting, Anita Kapros for the MS measurements, and Andras Lang and Daniel Horvath for helping 700 MHz NMR measurements. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. WoS:hiba:000463590400010 2019-04-21 12:29 cím nem egyezik Funding Agency and Grant Number: Eotvos Lorand University (ELTE); European UnionEuropean Commission; State of Hungary; European Regional Development FundEuropean Commission [VEKOP-2.3.2-16-2017-00014]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences Funding text: Open access funding provided by Eotvos Lorand University (ELTE). The authors wish to thank Dora K. Menyhard and Erno Keszei for consulting, Anita Kapros for the MS measurements, and Andras Lang and Daniel Horvath for helping 700 MHz NMR measurements. These research projects were supported by the European Union and the State of Hungary and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014). This paper was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (V. Farkas) and MedInProt Grant Facilitating Access to Instruments from the Hungarian Academy of Sciences. AB - The synthesis of α/β-chimeras comprises peptide bond formation from α- to β-, from β- to β-, and from β- to α-amino acid residues. The fine-tuned solid phase synthesis of –GXXG– chimera peptides containing the simplest achiral α-amino acid glycine and two cyclic SAAs of different ring size [X denoting cyclic β-Sugar Amino Acids (β-SAA)] is reported, variants containing Fmoc–RibAFU(ip)–OH a furanoid-, and Fmoc–GlcAPU(Me)–OH a pyranoid-type structural “Lego-element”. Systematic search for the best coupling strategy with both H–β-SAA–OHs is described, including the comparison of the different coupling reagents and conditions. Selecting the optimal reagent (from commonly used PyBOP, HATU and HOBt) was assisted by time-resolved 1H-NMR: formation and stability of the Fmoc protected active esters were compared. We found that PyBOP is the best choice for successfully coupling both H–β-SAA–OH prototypes. The present comparative results open a reasonable route for building efficiently various –β-SAA– containing homo- and heterooligomers. LA - English DB - MTMT ER - TY - JOUR AU - Nagy-Kanta, E. AU - Peterfia, B. AU - Hegedus, J. AU - Farkas, F. AU - Harmat, Z. AU - Farkas, Viktor AU - Batta, G. AU - Gaspari, Z. TI - Structural and functional characterization of the GKAP post-synaptic density scaffold protein JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 9 PY - 2019 SP - 255 EP - 255 PG - 1 SN - 2211-5463 UR - https://m2.mtmt.hu/api/publication/30847820 ID - 30847820 N1 - Supplement: 1 LA - English DB - MTMT ER - TY - CHAP AU - Farkas, Viktor AU - Jákli, Imre AU - Kardos, József AU - Vass, Elemér ED - Buday, László ED - Nyitray, László ED - Perczel, András TI - Elektron- és rezgési spektroszkópia a fehérjekutatásban T2 - Ezerarcú fehérjék PB - Semmelweis Kiadó és Multimédia Stúdió CY - Budapest SN - 9789633314586 PY - 2018 SP - 277 EP - 300 PG - 24 UR - https://m2.mtmt.hu/api/publication/30805932 ID - 30805932 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Schuster, Sabine AU - Biri-Kovács, Beáta AU - Bálint, Szeder AU - Farkas, Viktor AU - Buday, László AU - Szabó, Zsuzsanna AU - Halmos, Gábor AU - Mező, Gábor TI - Synthesis and in vitro biochemical evaluation of oxime bond-linked daunorubicin–GnRH-III conjugates developed for targeted drug delivery JF - BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY J2 - BEILSTEIN J ORG CHEM VL - 14 PY - 2018 SP - 756 EP - 771 PG - 16 SN - 1860-5397 DO - 10.3762/bjoc.14.64 UR - https://m2.mtmt.hu/api/publication/3363052 ID - 3363052 N1 - Funding Agency and Grant Number: European Union's Horizon research and innovation program under the Marie Sklodowska-Curie grant [642004]; Hungarian National Science Fund [OTKA K104045]; National Research, Development and Innovation Office [NKFIH K119552]; GINOP [2.3.2-15-2016-00043]; European Union; European Regional Development Fund Funding text: This project has received funding from the European Union's Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement No 642004, from the Hungarian National Science Fund (OTKA K104045) and National Research, Development and Innovation Office (NKFIH K119552). The work is also supported by the GINOP-2.3.2-15-2016-00043 (G.H.) project. The project is co-financed by the European Union and the European Regional Development Fund. The authors would like to acknowledge the help of Szilvia Bosze and Laszlo Kohidai in cell culture studies, Janos Gardi for his help in preparation of radioligand as well as Ildiko Szabo for providing triptorelin reagent. LA - English DB - MTMT ER -