Three Distinct d-Amino Acid Substitutions Confer Potent Antiangiogenic Activity on an Inactive Peptide Derived from a Thrombospondin-1 Type 1 Repeat

Mal II, a 19-residue peptide derived from the second type 1 properdin-like repeat of the antiangiogenic protein thrombospondin-1 (TSP-1), was inactive in angiogenesis assays. Yet the substitution of any one of three l -amino acids by their d -enantiomers conferred on this peptide a potent antiangiog...

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Veröffentlicht in:	Molecular pharmacology 1999-02, Vol.55 (2), p.332-338
Hauptverfasser:	Dawson, D W, Volpert, O V, Pearce, S F, Schneider, A J, Silverstein, R L, Henkin, J, Bouck, N P
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Amino Acid Sequence Amino Acids - chemistry Animals Cell Movement - drug effects Endothelial Growth Factors - pharmacology Endothelium, Vascular - cytology Endothelium, Vascular - drug effects Fibroblast Growth Factor 1 - pharmacology Fibroblast Growth Factor 2 - pharmacology Interleukin-8 - pharmacology Isoleucine - chemistry Lymphokines - pharmacology Mice Mice, Inbred C57BL Molecular Sequence Data Neovascularization, Pathologic - prevention & control Oligopeptides - chemistry Oligopeptides - pharmacology Platelet-Derived Growth Factor - pharmacology Rats Rats, Sprague-Dawley Repetitive Sequences, Nucleic Acid Sensitivity and Specificity Serine - chemistry Stereoisomerism Thrombospondin 1 - chemistry Thrombospondin 1 - pharmacology Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors
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