Dr. Kristaps Jaudzems

Vadošais pētnieks, laboratorijas vadītājs

E-pasts: kristaps.jaudzems@osi.lv
Tālrunis: (+371) 67014817

CV | Publikācijas

Curriculum Vitae

Dzimšanas dati 1984. gada 5. februāris, Rīga, Latvija

Izglītība

03/2011 Doktora grāds ķīmijā, Rīgas Tehniskā universitāte
Doktora darbs: “NMR studies of protein structure, function and ligand interactions”. Zinātniskie vadītāji: prof. E. Liepiņš un prof. K. Wüthrich
07/2008 Maģistra grāds ķīmijas tehnoloģijā, Rīgas Tehniskā universitāte
Maģistra darbs: “Proteīnu KMR spektroskopija un telpiskā uzbūve: DnaI un cikliskās Sortāzes A piemēri”. Zinātniskais vadītājs: prof. E. Liepiņš
07/2006 Bakalaura grāds ķīmijas tehnoloģijā, Rīgas Tehniskā universitāte
Bakalaura darbs: “Selektīvi aizsargātu glikozes-6-fosfāta analogu sintēze”. Zinātniskā vadītāja: prof. Ē. Bizdēna

Pētniecības pieredze

09/2017-tagad vadošais pētnieks, laboratorijas vadītājs Latvijas Organiskās sintēzes institūtā
09/2015-08/2017 Marie Skłodowska-Curie pēcdoktorantūras pētnieks Augsta lauka kodolu magnētiskās rezonanases centrā, Lionā, Francijā Dr. Anne Lesage grupā
11/2011-08/2015 vadošais pētnieks Latvijas Organiskās sintēzes institūtā
10-12/2014 vies-pētnieks Austrālijas Nacionālajā universitātē, Kanberā, Austrālijā. Apmācība bezšūnu proteīnu sintēzē un paramagnētiskajā KMR prof. Gottfried Otting vadībā
10-12/2012 vies-pētnieks Augsta lauka kodolu magnētiskās rezonanases centrā (Centre de RMN à Très Hauts Champs), Lionā, Francijā. Apmācība cietvielu KMR Dr. Guido Pintacuda vadībā
06-09/2011 vies-postdoks, The Scripps Research Institute, La Jolla, Kalifornijā, ASV prof. Kurt Wüthrich grupā
07/2010-05/2011 zinātniskais asistents Latvijas Organiskās sintēzes institūtā. Vadītājs: prof. Edvards Liepiņš
09/2008-06/2010 ārējais doktorants,The Scripps Research Institute, La Jolla, Kalifornija, ASV. Biomolekulu KMR pētījumi prof. Kurt Wüthrich vadībā
01/2007-08/2008 zinātniskais asistents Latvijas Organiskās sintēzes institūtā. Vadītājs: prof. Edvards Liepiņš
05/2006-12/2006 laborants Latvijas Organiskās sintēzes institūtā
09/2002-05/2006 laborants Rīgas Tehniskajā universitātē

Pasniedzēja pieredze

03/2018- asociētais profesors Latvijas Universitātē. Kursi: KMR spektroskopija, Dabasvielu ķīmija, Stereoķīmija
03/2018-01/2019 vies-asociētais profesors Rīgas Tehniskajā universitātē. Kursi: Fizikālās pētīšanas metodes, KMR spektroskopija
02/2012-02/2018 docents Rīgas Tehniskajā universitātē. Kursi: Fizikālās pētīšanas metodes, KMR spektroskopija
2013-2017 pasniedzējs Latvijas Universitātē. Kurss: KMR spektroskopija

Valodu zināšanas

Latviešu (dzimtā), angļu un vācu (tekoši), krievu (pamatzināšanas)

Apbalvojumi un stipendijas

12/2019 LZA īstenais loceklis
02/2018 LZA diploms par vienu no nozīmīgākajiem sasniegumiem Latvijas zinātnē 2017. gadā
12/2017 LZA korespondētājloceklis
10/2017 Eiropas Zinātņu un mākslu akadēmijas veicināšanas balva
09/2015-08/2017 Marie Skłodowska-Curie indivuālais grants
2013, 2015, 2017 RTU un A/S OlainFarm piešķirtā Solomona Hillera balva studiju noslēguma darba vadītājam
09/2010-05/2011 Eiropas Sociālā fonda stipendija
04/2009 Prof. Emīlijas Gudrinieces balva labākajam jaunajam zinātniekam ķīmijā
07/2006 A/S OlainFarm balva par labāko bakalaura darbu

Publikācijas

  1. Abelein A., Chen G., Kitoka K., Aleksis R., Oleskovs F., Sarr M., Landreh M., Pahnke J., Nordling K., Kronqvist N., Jaudzems K., Rising A., Johansson J., Biverstål H. High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Sci. Rep. (2020) 10: 235. DOI
  2. Brangulis K., Akopjana I., Petrovskis I., Kazaks A., Zelencova D., Jekabsons A., Jaudzems K., Tars K. BBE31 from the Lyme disease agent Borrelia burgdorferi, known to play an important role in successful colonization of the mammalian host, shows the ability to bind glutathione. Biochim. Biophys. Acta Gen. Subj. (2020) 1864: 129499. DOI
  3. Jaudzems K., Kurbatska V., Jēkabsons A., Bobrovs R., Rudevica Z., Leonchiks A. Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization. ACS Infect. Dis. (2020) 6: 186-194. DOI
  4. Brangulis K., Akopjana I., Petrovskis I., Kazaks A., Jekabsons A., Jaudzems K., Viksna A., Bertins M., Tars K. Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection. FEBS Lett. (2020) 594: 317-326. DOI
  5. Mohammadi P., Aranko A.S., Landowski C.P., Ikkala O., Jaudzems K., Wagermaier W., Linder M.B. Biomimetic composites with enhanced toughening using silk-inspired triblock proteins and aligned nanocellulose reinforcements. Sci. Adv. (2019) 5: eaaw2541. DOI
  6. Bobrovs R., Jaudzems K., Jirgensons A. Exploiting Structural Dynamics To Design Open-Flap Inhibitors of Malarial Aspartic Proteases. J. Med. Chem. (2019) 62: 8931-8950. DOI
  7. Gupta R., Zhang H., Lu M., Hou G., Caporini M., Rosay M., Maas W., Struppe J., Ahn J., Byeon I.L., Oschkinat H., Jaudzems K., Barbet-Massin E., Emsley L., Pintacuda G., Lesage A., Gronenborn A.M., Polenova T. Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. J. Phys. Chem. B (2019) 123: 5048-5058. DOI
  8. Jaudzems K., Polenova T., Pintacuda G., Oschkinat H., Lesage A. DNP NMR of biomolecular assemblies. J. Struct. Biol. (2019) 206: 90–98. DOI
  9. Zogota R., Kinena L., Withers-Martinez C., Blackman M.J., Bobrovs R., Pantelejevs T., Kanepe-Lapsa I., Ozola V., Jaudzems K., Suna E., Jirgensons A. Peptidomimetic plasmepsin inhibitors with potent anti-malarial activity and selectivity against cathepsin D. Eur. J. Med. Chem. (2019) 163: 344-352. DOI
  10. Kinena L., Leitis G., Kanepe‐Lapsa I., Bobrovs R., Jaudzems K., Ozola V., Suna E., Jirgensons A. Azole‐based non‐peptidomimetic plasmepsin inhibitors. Arch. Pharm. Chem. Life Sci. (2018) 351: 1800151. DOI
  11. Sarr M., Kronqvist N., Chen G., Aleksis R., Purhonen P., Hebert H., Jaudzems K., Rising A., Johansson J. A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein. FEBS J. (2018) 285: 1873–1885. DOI
  12. Rasina D., Stakanovs G., Borysov O.V., Pantelejevs T., Bobrovs R., Kanepe-Lapsa I., Tars K., Jaudzems K., Jirgensons A. 2-Aminoquinazolin-4(3H)-one based plasmepsin inhibitors with improved hydrophilicity and selectivity. Bioorg. Med. Chem. (2018) 26: 2488–2500. DOI
  13. Jaudzems K., Bertarello A., Chaudhari S.R., Pica A., Cala-De Paepe D., Barbet-Massin E., Pell A.J., Akopjana I., Kotelovica S., Gajan D., Ouari O., Tars K., Pintacuda G., Lesage A. Dynamic nuclear polarization enhanced biomolecular NMR spectroscopy at high magnetic field with fast magic-angle spinning. Angew. Chem. Int. Ed. (2018) 57: 7458-7462. DOI
  14. Charlton M.H., Aleksis R., Saint-Leger A., Gupta A., Loza E., Ribas de Pouplana L., Kaula I., Gustina D., Madre M., Lola D., Jaudzems K., Edmund G., Randall C.P., Kime L., O’Neill A.J., Goessens W., Jirgensons A., Finn P.W. N-Leucinyl Benzenesulfonamides as Structurally Simplified Leucyl-tRNA Synthetase Inhibitors. ACS Med. Chem. Lett. (2018) 9: 84–88. DOI
  15. Otikovs M., Andersson M., Jia Q., Nordling K., Meng Q., Andreas L.B., Pintacuda G., Johansson J., Rising A., Jaudzems K.. Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy. Angew. Chem. Int. Ed. (2017) 56: 12571–12575. DOI
  16. Cala-De Paepe D., Stanek J., Jaudzems K., Tars K., Andreas L.B., Pintacuda G. Is protein deuteration beneficial for proton detected solid-state NMR at and above 100 kHz magic-angle spinning? Solid State Nucl. Magn. Reson. (2017) 87: 126–136. DOI
  17. Aleksis R., Oleskovs F., Jaudzems K., Pahnke J., Biverstål H. Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity. Biochimie (2017) 140: 176-192. DOI
  18. Kronqvist N., Sarr M., Lindqvist A., Nordling K., Otikovs M., Venturi L., Pioselli B., Purhonen P., Landreh M., Biverstål H., Toleikis Z., Sjoberg L., Robinson C.V., Pelizzi N., Jornvall H., Hebert H., Jaudzems K., Curstedt T., Rising A., Johansson J. Efficient protein production inspired by how spiders make silk. Nat. Commun. (2017) 8: 15504. DOI (Full text)
  19. Stanek J., Andreas L.B., Jaudzems K., Cala D., Lalli D., Bertarello A., Schubeis T., Akopjana I., Kotelovica S., Tars K., Pica A., Leone S., Picone D., Xu Z.-Q., Dixon N.E., Martinez D., Berbon M., El Mammeri N., Noubhani A., Saupe S., Habenstein B., Loquet A., Pintacuda G. NMR spectroscopic assignment of backbone and side-chain protons in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils. Angew. Chem. Int. Ed. (2016) 55: 15504-15509. DOI
  20. Aleksis R., Jaudzems K., Muceniece R., Liepinsh E. Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions. Peptides (2016) 85: 56–62. DOI
  21. Recacha R., Jaudzems K., Akopjana I., Jirgensons A., Tars K. Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins. Acta Cryst. (2016) F72: 659–666. DOI
  22. Shishovs M., Rumnieks J., Diebolder C., Jaudzems K., Andreas L.B., Stanek J., Kazaks A., Kotelovica S., Akopjana I., Pintacuda G., Koning R.I., Tars K. Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages. J. Mol. Biol. (2016) 428: 4267–4279. DOI
  23. Andreas L.B., Jaudzems K., Stanek J., Lalli D., Bertarello A., Le Marchand T., Cala-De Paepe D., Kotelovica S., Akopjana I., Knott B., Wegner S., Engelke F., Lesage A., Emsley L., Tars K., Herrmann T., Pintacuda G. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR. Proc. Natl. Acad. Sci. USA (2016) 113: 9187–9192. DOI
  24. Tjernberg L.O., Rising A., Johansson J., Jaudzems K. and Westermark P. Transmissible amyloid. J. Intern. Med. (2016) 280: 153–163. DOI
  25. Rasina D., Otikovs M., Leitans J., Recacha R., Borysov O.V., Kanepe-Lapsa I., Domraceva I., Pantelejevs T., Tars K., Blackman M.J., Jaudzems K., Jirgensons A. Fragment-Based Discovery of 2-Aminoquinazolin-4(3H)-ones As Novel Class Nonpeptidomimetic Inhibitors of the Plasmepsins I, II, and IV. J. Med. Chem. (2016) 59: 374–387. DOI
  26. Recacha R., Leitans J., Akopjana I., Aprupe L., Trapencieris P., Jaudzems K., Jirgensons A., Tars K. Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors. Acta Cryst. (2015) F71: 1531–1539. DOI
  27. Brangulis K., Jaudzems K., Petrovskis I., Akopjana I., Kazaks A., Tars K. Structural and functional analysis of BB0689 from Borrelia burgdorferi, a member of the bacterial CAP superfamily. J. Struct. Biol. (2015) 192: 320–330. DOI
  28. Otikovs M., Chen G., Nordling K., Landreh M., Meng Q., Jörnvall H., Kronqvist N., Rising A., Johansson J., Jaudzems K. Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains. ChemBioChem (2015) 16: 1720–1724. DOI | Back Cover
  29. Chen W.N., Kuppan K.V., Lee M.D., Jaudzems K., Huber T., Otting G. O-tert-Butyltyrosine, an NMR tag for high-molecular weight systems and measurements of submicromolar ligand binding affinities. J. Am. Chem. Soc. (2015) 137: 4581–4586. DOI
  30. Andreas L.B., Le Marchand T., Jaudzems K., Pintacuda G. High-resolution proton-detected NMR of proteins at very fast MAS. J. Magn. Reson. (2015) 253: 36–49. DOI
  31. Jaudzems K., Pedrini B., Geralt M., Serrano P., Wüthrich K. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4. J. Biomol. NMR (2015) 61: 65–72. DOI
  32. Zhulenkovs D., Rudevica Z., Jaudzems K., Turks M., Leonchiks A. Discovery and structure–activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidase. Bioorg. Med. Chem. (2014) 22: 5988–6003. DOI
  33. Barbet-Massin E., Pell A.J., Retel J.S., Andreas L.B., Jaudzems K., Franks W.T., Nieuwkoop A.J., Hiller M., Higman V., Guerry P., Bertarello A., Knight M.J., Felletti M., Le Marchand T., Kotelovica S., Akopjana I., Tars K., Stoppini M., Bellotti V., Bolognesi M., Ricagno S., Chou J.J., Griffin R.G., Oschkinat H., Lesage A., Emsley L., Herrmann T., Pintacuda G. Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning. J. Am. Chem. Soc. (2014) 136: 12489–12497. DOI
  34. Andersson M., Chen G., Otikovs M., Landreh M., Nordling K., Kronqvist N., Westermark P., Jörnvall H., Knight S., Ridderstråle Y., Holm L., Meng Q., Jaudzems K., Chesler M., Johansson J., Rising A. Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains. PLoS Biol. (2014) 12: e1001921. DOI (Full text)
  35. Brangulis K., Petrovskis I., Kazaks A., Bogans J., Otikovs M., Jaudzems K., Ranka R., Tars K. Structural characterization of CspZ, a complement regulator factor H and FHL-1 binding protein from Borrelia burgdorferi. FEBS J. (2014) 281: 2613-2622. DOI
  36. Kronqvist N., Otikovs M., Chmyrov V., Chen G., Andersson M., Nordling K., Landreh M., Sarr M., Jörnvall H., Wennmalm S., Widengren J., Meng Q., Rising A., Otzen D., Knight S.D., Jaudzems K., Johansson J. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nat. Commun. (2014) 5: 3254. DOI
  37. Jaudzems K., Tars K., Maurops G., Ivdra N., Otikovs M., Leitans J., Kanepe-Lapsa I., Domraceva I., Mutule I., Trapencieris P., Blackman M.J., Jirgensons A. Plasmepsin Inhibitory Activity and Structure-Guided Optimization of a Potent Hydroxyethylamine-Based Antimalarial Hit. ACS Med. Chem. Lett. (2014) 5: 373-377. DOI
  38. Zhulenkovs D., Jaudzems K., Zajakina A., Leonchiks A. Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation. Biochem. Eng. J. (2014) 82: 200-209. DOI
  39. Aleksis R., Jaudzems K., Ivanova J., Žalubovskis R., Kalvinsh I., Liepinsh E. Reactivity of aziridine-2-carboxamide (Leakadine) with nucleophiles in aqueous solutions. Chem. Heterocycl. Comp. (2014) 49: 1589-1598. DOI
  40. Barbet-Massin E., Pell A.J., Jaudzems K., Franks W.T., Retel J.S., Kotelovica S., Akopjana I., Tars K., Emsley L., Oschkinat H., Lesage A., Pintacuda G. Out-and-back (13)C-(13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS. J. Biomol. NMR (2013) 56: 379-386. DOI
  41. Jaudzems K., Jia X., Yagi H., Zhulenkovs D., Graham B., Otting G., Liepinsh E. Structural Basis for 5′-End-Specific Recognition of Single-Stranded DNA by the R3H Domain from Human Sμbp-2. J. Mol. Biol. (2012) 424: 42-53. DOI
  42. Jaudzems K., Askarieh G., Landreh M., Nordling K., Hedhammar M., Jörnvall H., Rising A., Knight S.D., Johansson J. pH-Dependent Dimerization of Spider Silk N-Terminal Domain Requires Relocation of a Wedged Tryptophan Side Chain. J. Mol. Biol. (2012) 422: 477-487. DOI
  43. Johnson M.A., Jaudzems K., Wüthrich K. NMR structure of the SARS coronavirus nonstructural protein Nsp7 in solution at pH 6.5. J. Mol. Biol. (2010) 402: 619-628. DOI Full text
  44. Jaudzems K., Geralt M., Serrano P., Mohanty B., Horst R., Pedrini B., Elsliger M.-A., Wilson I.A., Wüthrich K. NMR structure of the protein NP_247299.1: comparison with the crystal structure. Acta Cryst. (2010) F66: 1367-1380. DOI (Full text)
  45. Mohanty B., Serrano P., Pedrini B., Jaudzems K., Geralt M., Horst R., Herrmann T., Elsliger M.-A., Wilson I.A., Wüthrich K. Comparison of NMR and crystal structures for the proteins TM1112 and TM1367. Acta Cryst. (2010) F66: 1381-1392. DOI (Full text)
  46. Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B., Horst R., Herrmann T., Elsliger M.-A., Wilson I.A., Wüthrich K. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites. Acta Cryst. (2010) F66: 1393-1405. DOI (Full text)
  47. Jaudzems K., Kuka J., Gutsaits A., Zinovjevs K., Kalvinsh I., Liepinsh E., Liepinsh E., Dambrova M. Inhibition of carnitine acetyltransferase by mildronate, a regulator of energy metabolism. J. Enz. Inhib. Med. Chem. (2009) 24: 1269-1275. DOI
  48. Loscha K.V., Jaudzems K., Ioannou C., Su X.-C., Hill F.R., Otting G., Dixon N.E., Liepinsh E. A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader. Nucleic Acids Res. (2009) 37: 2395-2404. DOI (Full text)

Patenti

  1. Kinena L., Ozola V., Suna E., Leitis G., Jirgensons A., Jaudzems K., Kanepe-Lapsa I., Domracheva I. Substituted aminoalkylazoles as malarial aspartic protease inhibitors. WO2017069601.
  2. Pelšs J., Domračeva I., Žalubovskis R., Jaudzems K. Derivatives of 2,6-diaza-bicyclo[2.2.2]octane-3,5-ditione as potential anti-cancer agents. LV15160.
  3. Jirgensons A., Domraceva I., Kanepe-Lapsa I., Rasina D., Jaudzems K., Otikovs M. Novel substituted 2-aminoquinazolin-4(3H)-one derivatives as malarial aspartic protease inhibitors. WO2015063544.
  4. Zhulenkovs D., Rudevica Z., Leonchiks A., Jaudzems K., Zicane D., Turks M. N-(3-hydroxy-5,7-dimethyladamantan-1-yl)-2-(3-oxobenzo[d]isothiazol-2(3h)-yl)acetamide as a novel inhibitor for staphylococcus aureus sortase a. EP2875816.
  5. Zhulenkovs D., Rudevica Z., Leonchiks A., Jaudzems K., Zicane D., Turks M. N’-(2-(3-oxobenzo[d]isothiazol-2(3h)-yl)acetyl)adamantane-1-carbohydrazide as a novel inhibitor for staphylococcus aureus sortase A. EP2875815.

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