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- W2051880607 abstract "Although not homologous to any known calmodulin binding sequences, αs1-casein 90−109 (RYLGYLEQLLRLKKYKVPQL), the initial seven residues corresponding to α-casein exorphin sequence, seems to be endowed with the molecular feature characteristic of this class of peptides: a higher proportion of basic and hydrophobic residues. αs1-Casein 90−109 was synthesized, and its calmodulin binding was examined. αs1-Casein 90−109 reduced the calmodulin-induced cyclic nucleotide phosphodiesterase activation at the comparable concentration to that previously reported for endogenous opioid peptides such as β-endorphin and dynorphin. αs1-Casein 90−109 as well as the endogenous opioid peptides shares the common structural motif matching for the interacting domains of calmodulin in the previously proposed complex model, suggesting that these opioid peptides may interact with calmodulin in a similar manner. Keywords: Calmodulin; casein; exorphin; complex model; opioid peptide" @default.
- W2051880607 created "2016-06-24" @default.
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- W2051880607 date "1997-05-01" @default.
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- W2051880607 title "Calmodulin Binding Peptide Comprising α-Casein Exorphin Sequence" @default.
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- W2051880607 doi "https://doi.org/10.1021/jf960720i" @default.
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