Structural comparison of μ-opioid receptor selective peptides confirmed four parameters of bioactivity
作者： Attila Borics , Géza Tóth
DOI: 10.1016/J.JMGM.2009.11.006
关键词:
摘要: Abstract Structural determinants of binding to the μ-opioid receptor, an important target in analgesia, attract great scientific attention. Many natural and synthetic peptides peptidomimetics were shown previously bind this receptor selectively but there is no consensus about structure responsible for biological activity. No high resolution available site ligands not exactly known. However, with similar affinity selectivity should possess at least one common structural feature. Comparative analysis such ligands, considering adequate representation conditions, may reveal key features bioactivity. In study ten DAMGO, Tyr-W-MIF-1, morphiceptin, endomorphin-1 2 their analogues, possessing different selectivity, examined using molecular dynamics. Conformational preference these molecules was determined H O DMSO along properties proposed be binding. Four requirements confirmed important, providing a possible model Simultaneous fulfillment results most likely receptor.
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