Aladan {β-[6＇-（N,N-dimethyl）amino-2＇-naphthoyl]alanine} and aladan-containing cyclodecapeptide [Ald^6]loloatin C were synthesized. The properties of their fluorescent behaviours both in aqueous buffer and micelle...Aladan {β-[6＇-（N,N-dimethyl）amino-2＇-naphthoyl]alanine} and aladan-containing cyclodecapeptide [Ald^6]loloatin C were synthesized. The properties of their fluorescent behaviours both in aqueous buffer and micelles created by sodium dodecylsulfate （SDS） and dodecylphosphorylcholine （DPC） were further investigated. It was found that in either of micelle systems, [Ald^6]loloatin C possesses red-shift emission maximum wavelength and higher quantum yield. This property could be useful in the research of peptide-cell membrane interaction.展开更多
An unnatural amino acid, β-[6′-(N, N-dimethyl)amino-2′-naphthoyl]alanine (Ald) showing polarity-sen sitive fluorescence characteristics, was synthesized. A thorough Ald-scan of dynorphin A (Dyn A), the putative end...An unnatural amino acid, β-[6′-(N, N-dimethyl)amino-2′-naphthoyl]alanine (Ald) showing polarity-sen sitive fluorescence characteristics, was synthesized. A thorough Ald-scan of dynorphin A (Dyn A), the putative endogenous ligand for κ opioid receptors, was then performed. Replacement of the amino acid residues in positions 5, 8, 10, 12 or 14 of Dyn A(1-13)-NH2 with Ald resulted in compounds that had almost equal κ binding affinity compared with that of the parent compound; on the other hand, substi-tution of residues in position 1 or 4 with Ald decreased κ-receptor binding affinity. These results indi-cate that Tyr and Phe in Dyn A are very important for maintaining its κ-opioid activity. Evidence from receptor binding assay clearly displays that [Ald5]Dyn A(1-13)-NH2 is a highly selective κ-opioid re-ceptor agonist. An evaluation of the interaction of Ald-containing Dyn A(1-13)-NH2 analogues with SDS and DPC micelles was also performed. Interestingly, [Ald1]Dyn A(1-13)-NH2 and [Ald4]Dyn A(1-13)-NH2 showed quite different fluorescence emission maxima in SDS and DPC micelles. This indicates that both peptides are sensitive to electronic properties of the polar surface of the micelles.展开更多
文摘Aladan {β-[6＇-（N,N-dimethyl）amino-2＇-naphthoyl]alanine} and aladan-containing cyclodecapeptide [Ald^6]loloatin C were synthesized. The properties of their fluorescent behaviours both in aqueous buffer and micelles created by sodium dodecylsulfate （SDS） and dodecylphosphorylcholine （DPC） were further investigated. It was found that in either of micelle systems, [Ald^6]loloatin C possesses red-shift emission maximum wavelength and higher quantum yield. This property could be useful in the research of peptide-cell membrane interaction.
基金Supported by the National Natural Science Foundation of China (Grant No. 30672560)the Ascended Project for Natural Scientific Research of Universities in Guangdong Province (Grant No. 05Z012)
文摘An unnatural amino acid, β-[6′-(N, N-dimethyl)amino-2′-naphthoyl]alanine (Ald) showing polarity-sen sitive fluorescence characteristics, was synthesized. A thorough Ald-scan of dynorphin A (Dyn A), the putative endogenous ligand for κ opioid receptors, was then performed. Replacement of the amino acid residues in positions 5, 8, 10, 12 or 14 of Dyn A(1-13)-NH2 with Ald resulted in compounds that had almost equal κ binding affinity compared with that of the parent compound; on the other hand, substi-tution of residues in position 1 or 4 with Ald decreased κ-receptor binding affinity. These results indi-cate that Tyr and Phe in Dyn A are very important for maintaining its κ-opioid activity. Evidence from receptor binding assay clearly displays that [Ald5]Dyn A(1-13)-NH2 is a highly selective κ-opioid re-ceptor agonist. An evaluation of the interaction of Ald-containing Dyn A(1-13)-NH2 analogues with SDS and DPC micelles was also performed. Interestingly, [Ald1]Dyn A(1-13)-NH2 and [Ald4]Dyn A(1-13)-NH2 showed quite different fluorescence emission maxima in SDS and DPC micelles. This indicates that both peptides are sensitive to electronic properties of the polar surface of the micelles.
