@article{MTMT:34781847,
	title = {Unveiling the Oxazolidine Character of Pseudoproline Derivatives by Automated Flow Peptide Chemistry},
	url = {https://m2.mtmt.hu/api/publication/34781847},
	author = {Szaniszló, Szebasztián and Csámpai, Antal and Horváth, Dániel and Tomecz, Richárd and Farkas, Viktor and Perczel, András},
	doi = {10.3390/ijms25084150},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34781847},
	issn = {1661-6596},
	abstract = {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.},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Szaniszló, Szebasztián/0000-0002-8929-0635; Csámpai, Antal/0000-0003-2107-7309; Horváth, Dániel/0000-0001-8239-3933; Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34765015,
	title = {Influence of Aza-Glycine Substitution on the Internalization of Penetratin},
	url = {https://m2.mtmt.hu/api/publication/34765015},
	author = {Tarchoun, Karima and Soltész, Dóra and Farkas, Viktor and Lee, Ho-Jin and Szabó, Ildikó and Bánóczi, Zoltán},
	doi = {10.3390/pharmaceutics16040477},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {16},
	unique-id = {34765015},
	issn = {1999-4923},
	abstract = {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.},
	year = {2024},
	eissn = {1999-4923},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Lee, Ho-Jin/0000-0002-3251-4984; Szabó, Ildikó/0000-0002-9844-7841; Bánóczi, Zoltán/0000-0003-1880-4042}
}

@article{MTMT:34398184,
	title = {Synthesis of small protein domains by automated flow chemistry},
	url = {https://m2.mtmt.hu/api/publication/34398184},
	author = {Ferentzi, Kristóf and Nagy-Fazekas, Dóra and Farkas, Viktor and Perczel, András},
	doi = {10.1039/D3RE00324H},
	journal-iso = {REACT CHEM ENG},
	journal = {REACTION CHEMISTRY & ENGINEERING},
	volume = {9},
	unique-id = {34398184},
	issn = {2058-9883},
	abstract = {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...},
	year = {2024},
	eissn = {2058-9883},
	pages = {58-69},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:34014650,
	title = {Improved Acylation of Pseudoproline: Masked Threonine in Flow Peptide Chemistry},
	url = {https://m2.mtmt.hu/api/publication/34014650},
	author = {Szaniszló, Szebasztián and Ferentzi, Kristóf and Perczel, András and Farkas, Viktor},
	doi = {10.1021/acs.oprd.3c00029},
	journal-iso = {ORG PROCESS RES DEV},
	journal = {ORGANIC PROCESS RESEARCH & DEVELOPMENT},
	volume = {27},
	unique-id = {34014650},
	issn = {1083-6160},
	year = {2023},
	eissn = {1520-586X},
	pages = {1053-1060},
	orcid-numbers = {Szaniszló, Szebasztián/0000-0002-8929-0635; Perczel, András/0000-0003-1252-6416; Farkas, Viktor/0000-0002-8815-2783}
}

@article{MTMT:34034758,
	title = {Self-assembled and membrane active beta[sup]3 [/sup]-peptides: from design to application},
	url = {https://m2.mtmt.hu/api/publication/34034758},
	author = {Szigyarto, Imola and El, Battioui Kamal and Farkas, Viktor and Wacha, András Ferenc and Mihaly, Judith and Schlosser, Gitta (Vácziné) and Juhasz, Tunde and Románszki, Loránd and Varga, Zoltan and Mandity, Istvan and Beke-Somfai, Tamas},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {28},
	unique-id = {34034758},
	issn = {1075-2617},
	keywords = {Biochemistry & Molecular Biology},
	year = {2022},
	eissn = {1099-1387},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Wacha, András Ferenc/0000-0002-9609-0893; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133}
}

@article{MTMT:34034560,
	title = {Early stage amyloid formation probed: what makes cross-beta spine stable},
	url = {https://m2.mtmt.hu/api/publication/34034560},
	author = {Bencs, Fruzsina and Farkas, Viktor and Perczel, András},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {28},
	unique-id = {34034560},
	issn = {1075-2617},
	keywords = {Biochemistry & Molecular Biology},
	year = {2022},
	eissn = {1099-1387},
	orcid-numbers = {Bencs, Fruzsina/0009-0003-9246-2228; Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:33155481,
	title = {Succinct Amyloid and Nonamyloid Patterns in Hexapeptides},
	url = {https://m2.mtmt.hu/api/publication/33155481},
	author = {Keresztes, László and Szögi, Evelin and Varga, Bálint and Farkas, Viktor and Perczel, András and Grolmusz, Vince},
	doi = {10.1021/acsomega.2c02513},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {7},
	unique-id = {33155481},
	issn = {2470-1343},
	year = {2022},
	eissn = {2470-1343},
	pages = {35532-35537},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416; Grolmusz, Vince/0000-0001-9456-8876}
}

@misc{MTMT:32725488,
	title = {Succinct Amyloid and Non-Amyloid Patterns in Hexapeptides},
	url = {https://m2.mtmt.hu/api/publication/32725488},
	author = {Laszlo, Keresztes and Evelin, Szogi and Balint, Varga and Farkas, Viktor and Perczel, András and Grolmusz, Vince},
	unique-id = {32725488},
	abstract = {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.},
	year = {2022},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416; Grolmusz, Vince/0000-0001-9456-8876}
}

@article{MTMT:32467225,
	title = {Application of Sugar Amino Acids: Flow chemistry used for α/β‐chimera synthesis},
	url = {https://m2.mtmt.hu/api/publication/32467225},
	author = {Goldschmidt Gőz, Viktória and Duong, Kim Hoang Yen and Horváth, Dániel and Ferentzi, Kristóf and Farkas, Viktor and Perczel, András},
	doi = {10.1002/ejoc.202100943},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2021},
	unique-id = {32467225},
	issn = {1434-193X},
	year = {2021},
	eissn = {1099-0690},
	pages = {6071-6083},
	orcid-numbers = {Horváth, Dániel/0000-0001-8239-3933; Farkas, Viktor/0000-0002-8815-2783; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32152017,
	title = {Characterization of the interaction between Shank-PDZ and GKAP-GH1 domains},
	url = {https://m2.mtmt.hu/api/publication/32152017},
	author = {Santa, A. and Keresztes, M. and Nagy-Kanta, E. and Hegedus, J. and Farkas, Viktor and Batta, Gyula and Gáspári, Zoltán and Peterfia, B.},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {11},
	unique-id = {32152017},
	issn = {2211-5463},
	year = {2021},
	eissn = {2211-5463},
	pages = {200-201},
	orcid-numbers = {Farkas, Viktor/0000-0002-8815-2783; Batta, Gyula/0000-0002-0442-1828}
}