Proteolytically stable peptides by incorporation of α-Tfm amino acids

A series of model peptides containing α‐trifluoromethyl‐substituted amino acids in five different positions relative to the predominant cleavage site of the serine protease α‐chymotrypsin was synthesized by solution methods to investigate the influence of α‐Tfm substitution on the proteolytic stabil...

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Veröffentlicht in:	Journal of peptide science 1997-05, Vol.3 (3), p.157-167
Hauptverfasser:	Koksch, Beate, Sewald, Norbert, Hofmann, Hans-Jörg, Burger, Klaus, Jakubke, Hans-Dieter
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminoisobutyric Acids Chymotrypsin - metabolism Cα,α‐disubstituted glycines Dimethyl Sulfoxide Fluorine - chemistry Methylation Models, Molecular Peptides - chemical synthesis Peptides - chemistry Peptides - metabolism Protein Engineering - methods proteolytic stability α-chymotrypsin α-disubstituted glycines α-trifluoromethyl substituted amino acids
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