- Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus
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Lysostaphin (EC. 3.4.24.75) is a protein secreted by Staphylococcus simulans biovar staphylolyticus and has been shown to be active against methicillin resistant S. aureus (MRSA). The design and synthesis of three internally quenched substrates for lysost
- Warfield, Rachel,Bardelang, Philip,Saunders, Helen,Chan, Weng C.,Penfold, Christopher,James, Richard,Thomas, Neil R.
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p. 3626 - 3638
(2008/10/09)
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- SYNTHESIS OF A CYCLIC OCTAPEPTIDE
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The cyclic octapeptide cyclo-((L-Lys(Z))2-Gly-(L-Phe)2-(Gly)3) (13) was synthesized as an ionophore model. And transport of L-Phe-OMe*HCl through an organic liquid membrane mediated by (13) is reported.
- Katagi, Toyoshi,Kataoka, Hiromi
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p. 2109 - 2116
(2007/10/02)
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- STUDIES OF BITTER PEPTIDES FROM CASEIN HYDROLYZATE - VI. SYNTHESES AND BITTER TASTE OF BPIc (VAL-TYR-PRO-PHE-PRO-PRO-GLY-ILE-ASN-HIS) AND ITS ANALOGS AND FRAGMENTS.
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In order to investigate the relationship between chemical structure and bitter taste, the bitter peptide BPIc (Val-Tyr-Pro-Phe-Pro-Pro-Gly-Ile-Asn-His) isolated from casein hydrolyzate by Minamiura et al. and its analogs and fragments were synthesized. BPIc, whose threshold value of bitter taste was 0. 05 mm, was found to be one of the most bitter compounds, like quinine and phenylthiourea. However, left bracket Gly**5**,**6 right bracket - and left bracket Gly**9**,**1**0 right bracket -BPIc, and N-terminal octa- and heptapeptide fragments of BPIc possessed much weaker bitterness than BPIc. The results suggested that 5,6-proline and the basic nature of C-terminal are necessary for the strong bitterness exhibited by BPIc.
- Kanehisa
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