Cyclic, Linear, Cycloretro-Isomer, and Cycloretro-Inverso Peptides Derived from the C-Terminal Sequence of Bradykinin as Substrates or Inhibitors of Serine and Cysteine Proteases

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dc.contributor.author Lima, Aurelio Resende [UNIFESP]
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Juliano, Maria Aparecida [UNIFESP]
dc.date.accessioned 2016-01-24T12:37:10Z
dc.date.available 2016-01-24T12:37:10Z
dc.date.issued 2004-05-01
dc.identifier http://dx.doi.org/10.1023/B:JOPC.0000027853.93513.34
dc.identifier.citation Protein Journal. New York: Springer, v. 23, n. 4, p. 287-294, 2004.
dc.identifier.issn 1572-3887
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/27757
dc.description.abstract We investigated the inhibition of trypsin, human tissue (hK1) and human plasma kallikrein (HuPK), papain, and cathepsin L, B, and X by synthetic cyclic, cycloretro-isomer, cycloretro-inverso, and linear peptides derived from the C-terminal sequence of bradykinin. c(FSPFRG) and Ac-FSPFRG-NH(2) were taken as the references for cyclic and linear peptides, respectively. Longer and more flexible analogs of them with addition of 2, 3, or 4 Gly and cycloretro-isomer and cycloretro-inverso analogs of c(FSPFRG) and c(GGGFSPFRG) were obtained and assayed. the susceptibility to hydrolysis of the peptides to all proteases was also examined. the highest affinities were found for c(FSPFRG) with hK1, Ac-GGFSPFRG-NH(2) with HuPK, and psi (NHCO) c(fspfrG) with cathepsin L. the K(i) values for cathepsin B and X with cyclic peptides were lower than those of linear peptides. the serine proteases hydrolyzed all linear and cyclic peptides, except c(FSPFRG) and c(GFSPFRG). the cysteine proteases hydrolyzed only the linear peptides, which were poor substrates. Although the K(i) values obtained in the current work were in the mu M range, the cyclic and cycloretro-inverso peptides seem to be a promising approach to develop efficient and resistant to hydrolysis inhibitors for the kallikreins and lysosomal cysteine proteases. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Human Frontiers for Science Progress
dc.format.extent 287-294
dc.language.iso eng
dc.publisher Springer
dc.relation.ispartof Protein Journal
dc.rights Acesso restrito
dc.subject Cathepsin B en
dc.subject cathepsin L en
dc.subject cathepsin X en
dc.subject kallikrein en
dc.subject peptides en
dc.subject trypsin en
dc.title Cyclic, Linear, Cycloretro-Isomer, and Cycloretro-Inverso Peptides Derived from the C-Terminal Sequence of Bradykinin as Substrates or Inhibitors of Serine and Cysteine Proteases en
dc.type Artigo
dc.rights.license http://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-0404420 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-0404420 São Paulo, Brazil
dc.description.sponsorshipID Human Frontiers for Science Progress: RG 00043/2000-M
dc.identifier.doi 10.1023/B:JOPC.0000027853.93513.34
dc.description.source Web of Science
dc.identifier.wos WOS:000208031900006



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