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Luis Moroder

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Luis Moroder (nasciù ai 6 de dezëmber 1940) ie n studiëus de chimica dl peptide y ie stat un di primes a nrescì sun i ormons peptide y coche chisc va adum cun la membranes dla zeles.

Do chë iel jit inant a nrescì autri sitemes dla natura che à mpurtanza tla medejina. Chisc ie i inibitëures dl protein, i collagens y la proteines sintetiches.

De si tuedes ie de mpurtanza che l à purtà pro che chisc sistems ie uni adurvei y svilupei tla chimica organica, tla biofisica y tla biologia moleculera.

E4l à laurà pea tl stude publicà te cin libri de Houben-Weyl Methods of Organic Chemistry, Synthesis of Peptides and Peptidomimetics. Dal ann 2008 ie Luis Moroder l diretëur de Journal of Peptide Science la plata ufiziela dla European Peptide Society.[1]

Si vita scoles y cariera

Luis Moroder à studià chimica tla università de Padua y ie deventà dutor l ann 1965 cun na tesis sun la sintesa dl S-peptide dla ribonuclease A lauran tl lauratuere de Ernesto Scoffone tl istitut de chimica organica.[2] L ann 1968 iel jit pra la grupa de Klaus H. Hofmann tla University of Pittsburgh per lauré sun la sintesa chemica dl hormon adrenocorticotropich .[3]

Moroder à fat si abilitazion l ann 1971 tla Università de Padua sun la chimica di prudoc naturei.


L ann 1975 iel deventà cunlauradëur tl Max-Planck-Institut für Biochemie (MPIB) a Martinsried sota a Erich Wünsch [de].

Ti ani 1991 nchin 2008 iel stat diretëur dl lauratuere per chimica bioorganica tl Istitut Max Planck a Martinsried. Dal 1994 iel nce profesëur tla Università de Minca.

Nrescides

Moroder à scumencià si tuedes sun i peptides cun la sintesa dl S-peptide dl ribonuclease Ay cun studiesdl complex protein-peptide. L fova una dla prima desmustrazion dl prinzip tlé-śaradura dl rezeptor peptide ormonn.

Ël à laurà sun la sintesa dl adrenocorticotropin radioactiv, lëur che fova l prim ejëmpl de stude de na sintesa di ormonns peptide dla persona.

Si lëur tl Max Planck Institut a Martinsried fova dl viëres dl sistem gastrin/cholecystokinin, che à mustra coche l ormonn vën recunesciù dal rezeptor passan tres la membrana.

Plu inant se al nteressà a sistemes dla biologia y tla medejina plu cumplichei.

Ël se à cruzià de questions fundamenteles che reverda l lubrì dla proteines.



Moroder's work at the Max Planck Institute for Biochemistry in Martinsried was initially focused on the g system, revealing the mechanism for the membrane-bound pathway of hormone recognition by the receptors.[4] In parallel, he worked on synthetic methods in peptide and protein chemistry such as the introduction of di-<i id="mwQA">tert</i>-butyl dicarbonate as a general and widely used reagent in peptide chemistry,[5] regioselective assembly of cystine-rich peptides,[6] and the synthesis of highly robust disulfide/diselenide scaffolds.[7]

In the later phase of his research, Moroder became increasingly interested in the study of more complex biological and medical systems by chemical means. For example, he addressed fundamental questions of the kinetics of protein folding[8] and actively contributed to the design and synthesis of enzyme inhibitors involved in various diseases, including cancer.[9] In the 1990s Luis Moroder and Robert Huber supported Nediljko Budisa in establishing genetic code engineering in Germany - a research area that merges chemical syntheses with biological complexities in the form of chemical synthetic biology (Xenobiology).[10][11]

Premi y uneranzes

  • 1995: bedaia Max-Bergmann dl Max Bergmann Kreis[12]
  • 2004: premi Josef Rudinger dla European Peptide Society[13]
  • 2011: Dutor honoris causa dla Università Cergy-Pontoise, Paris[2]
  • 2018: premi Akabori Memorial dla Japanese Peptide Society[14]
  • 2020: premi Ernesto Scoffone dla Italian Peptide Society[15]

Vita persunela

Luis Moroder ie cresciù su te Gherdëina. E4l ie l mut de Agnes Kostner de Stlujuc y de Heinrich Moroder de Doss che l tulova for pea a fe nrescides sun i minerai y curëc. Ël ie maridà cun Anne Marie Hellrigl. Ëi à na muta.


Publicazions


669 publications scientifiches.

Notes

  1. ↑ "Luis Moroder | Max Planck Institute of Biochemistry". Max Planck Institute. Trat ite ai 2021-08-20.
  2. ↑ 2,0 2,1 "Detailed CV - cv_moroder.pdf" (PDF). Max Planck Institute. Trat ite ai 2021-08-20.
  3. ↑ Moroder, L.; Hofmann, K. (1970). "Studies on polypeptides. XLVI. Synthesis of a stably labeled, biologically active adrenocorticotropin fragment". J Med Chem. 13 (5): 839–843. doi:10.1021/jm00299a010. PMID 4318767.
  4. ↑ Moroder, L.; Romano, R.; Guba, W.; Mierke, D. F.; Kessler, H.; Delporte, C.; Winand, J.; Christophe, J. (1993). "New evidence for a membrane-bound pathway in hormone receptor binding". Biochemistry. 32 (49): 13551–13559. doi:10.1021/bi00212a022. PMID 7504952.
  5. ↑ Moroder, L.; Hallett, A.; Wünsch, E.; Keller, O.; Wersin, G. (1976). "Di-tert-Butyldicarbonat: ein vorteilhaftes Reagenz zur Einführung der tert-Butyloxycarbonyl-Schutzgruppe" [Di-tert-butyl-dicarbonate, a useful tert-butyloxycarbonylating reagent]. Hoppe-Seyler's Z. Physiol. Chem. 357 (11): 1651–1653. doi:10.1515/bchm2.1976.357.2.1651. PMID 1002132.
  6. ↑ Moroder, L.; Musiol, H.-J.; Götz, M.; Renner, C. (2005). "Synthesis of single- and multiple-stranded cystine-rich peptides". Biopolymers. 80 (2–3): 85–97. doi:10.1002/bip.20174. PMID 15612050.
  7. ↑ Besse, D.; Siedler, F.; Diercks, T.; Kessler, H.; Moroder, L. (1997). "The redox potential of selenocystine in unconstrained cyclic peptides". Angew. Chem. Int. Ed. 36 (8): 883–885. doi:10.1002/anie.199708831.
  8. ↑ Bredenbeck, J.; Helbing, J.; Sieg, A.; Schrader, T.; Zinth, W.; Wachtveitl, J.; Renner, C.; Behrendt, R.; Moroder, L.; Hamm, P. (2003). "Picosecond conformational transition and equilibration of a cyclic peptide". Proc. Natl. Acad. Sci. USA. 100 (11): 6452–6457. Bibcode:2003PNAS..100.6452B. doi:10.1073/pnas.1036583100. PMC 164467. PMID 12736378.
  9. ↑ Loidl, G.; Groll, M.; Musiol, H.-J.; Huber, R.; Moroder, L. (1999). "Bivalency as a principle for proteasome inhibition". Proc. Natl. Acad. Sci. USA. 96 (10): 5418–5422. Bibcode:1999PNAS...96.5418L. doi:10.1073/pnas.96.10.5418. PMC 21874. PMID 10318898.
  10. ↑ Budisa, N.; Minks, C.; Medrano, F. J.; Lutz, J.; Huber, R.; Moroder, L. (1998). "Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant of annexin V". Proc. Natl. Acad. Sci. USA. 95 (2): 455–459. Bibcode:1998PNAS...95..455B. doi:10.1073/pnas.95.2.455. PMC 18441. PMID 9435213.
  11. ↑ Moroder, L.; Budisa, N. (2010). "Synthetic biology of protein folding". ChemPhysChem. 11 (6): 1181–1187. doi:10.1002/cphc.201000035. PMID 20391526.
  12. ↑ "Max-Bergmann-Medaille - Max Bergmann Kreis e.V." Max Bergmann Kreis e.V. Trat ite ai 2021-08-20.
  13. ↑ "Josef Rudinger Memorial Award - European Peptide Society". European Peptide Society. May 18, 2016. Trat ite ai 2021-08-20.
  14. ↑ "Akabori Memorial Award | The Japanese Peptide Society". Japanese Peptide Society. Trat ite ai 2021-08-20.
  15. ↑ "Votazioni on line, Premio Scoffone per l'anno 2020: estensione voto al 20 Aprile 2020". Italian Peptide Society. Trat ite ai 2021-08-20.
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