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Professor Luiz Juliano
Department of Biophysics
Universidade Federal de Sao Paulo, Escola Paulista de Medicina
Rua Tres de Maio, 100, 04044-020 Sao Paulo, Brazil
Email: juliano.biof@epm.br
Tel: 55-11-5539-0809
Fax: 55-11-5575-9617

We have been working in the organic synthesis of peptides and amino acids aimed at the study of proteases. Series of internally quenched fluorescent peptides having as donnor-receptor fluorescent pair ortho-aminobenzoic acid (Abz) and N-[2,4-dinitrophenyl]-ethylenediamine (EDDnp), respectively we have systematically synthesized and used to study the specificity of proteases. Peptide libraries in solution or attached in polymeric supported have being also used to study protease specicity. The following proteolytic enzymes are of our interest: a) Serine proteases as tissue and plasma kallikreins, cathepsin G, human tissue kallikreins; b) Lisosomal cathepisn F, K, H, S, V and X; c) Proteases from tropical parasite diseases as leishmania and malaria, and from virus as dengue, yelow fever and human hepatitis C; d) Endooligopeptidases; e) Metalloproteases as angiotensin converting enzyme and PHEX, 24.11 and 24.15); f) convertases (Kex2, PC1, PC2, PC5/6 and furin). Non-natural amino acids were incorporated in peptides, and modifications on their peptide bond performed in order to obtain specific substrates and inhibitors for the proteases we are studying.
Cell proteolysis in in situ using the substrates and inhibitors are being developed. In addition, we are proposing to establish a cell culture laboratory for these studies as well as to produce most of the proteases that we are proposing to study.
Boris Turk
Dieter Bromme
Dr. Michael Blaber
Edward Sturrock
Francis Jean
Graham H. Coombs
Guy Boileau
Jorge Arevalo
Laszlo Polgar
Louis B. Hersh
Norma Andrews
Philip J. Rosenthal
Paul RYoung
Rory Morhi
Vincenzo Santagada
Alves MF, Puzer L, Cotrin SS, Juliano MA, Juliano L, Bromme D, Carmona AK. (2003) S3 to S3' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates. Biochem J 373: 981-986.

Hemerly JP, Oliveira V, Del Nery E, Morty RE, Andrews NW, Juliano MA, Juliano L. (2003) Subsite specificity (S3, S2, S1, S2 and S3 ) of Oligopeptidase B from Trypanosoma cruzi and Trypanosoma brucei using Fluorescent-Quenched Peptides: A comparative study and identification of specific carboxypeptidase activity. Biochem J 373: 933-938.

Cezari MHS, Puzer L, Juliano MA, Carmona AK and Juliano L. (2002) Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides. Biochemical J 368:365-369.

Song ES, Juliano MA, Juliano L, Hersh LB. (2003) Substrate activation of insulin degrading enzyme (Insulysin): A potential target for drug development. J Biol Chem. 278: 49789-49794

Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L. (2003) Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J Biol Chem. 278: 48786-48793

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