Amino acids with amphiphilic side chains: Deltorphin analogues with Phe3 replaced by all ?-hydroxyphenylalanine diastereoisomers
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/BF00119153.pdf
Reference7 articles.
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4. Proceedings of the 2nd Japan Symposium on Peptide Chemistry;A. Misicka,1993
5. Bergmann, E.D., Bendas, H. and Resmick, C., J. Chem. Soc., (1953) 2564.
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1. The biological consequences of replacing hydrophobic amino acids in deltorphin I with amphiphilic α-hydroxymethylamino acids;The Journal of Peptide Research;2003-05-28
2. Synthesis, biology, NMR and conformation studies of the topographically constrained δ-opioid selective peptide analogs of [β-iPrPhe3 ]deltorphin I;The Journal of Peptide Research;2001-04
3. Synthesis and binding properties of endomorphin-2 analogs containing α-hydroxymethyl amino acids;Letters in Peptide Science;2000-03
4. Analogs of arginine vasopressin modified in position 3 with (R)-α- hydroxymethylphenylalanine;The Journal of Peptide Research;1999-05
5. Biological consequences of the incorporation of amphiphilic amino acids into opioid peptide sequences;Letters in Peptide Science;1998-10
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