期刊
LETTERS IN PEPTIDE SCIENCE
卷 7, 期 2, 页码 93-96出版社
KLUWER ACADEMIC PUBL
DOI: 10.1007/BF02443567
关键词
amphiphilic amino acid; endomorphin-2; alpha-hydroxymethylphenylalanine; alpha-hydroxymethyltyrosine
Novel endomorphin-2 analogs containing the unusual amphiphilic amino acid (R)- and (S)-alpha-hydroxymethyltyrosine in position 1 and (R)- and (S)-alpha-hydroxymethylphenylalanine in the positions 3 and 4 were synthesized via the solid-phase method. The binding characteristics of the synthetic analogs may suggest that alpha-hydroxymethyl substitution of amino acid residues influences the conformation of a peptide much more than simply increasing the local amphiphilic character of the peptide.
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