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In vitro evaluation of leptin fragments activity on the ob receptor
Author(s) -
de Oliveira Vani Xavier,
Fázio Marcos Antonio,
Santos Edson Lucas,
Pesquero João bosco,
Miranda Antonio
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.957
Subject(s) - leptin , chemistry , leptin receptor , in vitro , dimer , receptor , peptide , molecule , stereochemistry , disulfide bond , medicine , biochemistry , endocrinology , biology , obesity , organic chemistry
In an attempt to identify regions in the leptin molecule responsible for its bioactivity, we tested six related‐leptin peptide fragments denoted: Ac‐hLEP 23–47 ‐NH 2 ( I ), Ac‐hLEP 48–71 ‐NH 2 ( II ), Ac‐hLEP 72–88 ‐NH 2 ( III ), Ac‐hLEP 92–115 ‐NH 2 ( IV ), Ac‐[Ser 117 ]‐hLEP 116–140 ‐NH 2 ( V ), Ac‐hLEP 141–164 ‐NH 2 ( VI ) and their correspondent disulfide bridged dimer forms. The activity of the fragments was evaluated in comparision to leptin, by their ability to interact with leptin receptor using a cytosensor microphysiometer. Our results indicated that the fragments IV and V and [D‐Leu 4 ]‐OB 3 and its human sequence analog were recognized by leptin receptor present in HP‐75 cells, in agreement with the results obtained by other workers, validating that this region of the molecule contain the functional epitope of the leptin molecule. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.