A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity.

Abstract:

:The first recombinant endostatin that elicited strong antitumor activity was expressed in Escherichia coli and administered as a suspension. Under these conditions, the protein retained its full antiangiogenic activity. Lack of requirement for a folded structure prompted us to investigate antitumor properties of synthetic peptides corresponding to different regions of endostatin. Here, we show that the entire antitumor, antimigration, and antipermeability activities of endostatin are mimicked by a 27-amino-acid peptide corresponding to the NH2-terminal domain of endostatin. This peptide contains three histidines that are responsible for zinc binding. Mutations of the zinc-binding histidines abolished its antitumor and antimigration activities, but not antipermeability properties.

journal_name

Cancer Res

journal_title

Cancer research

authors

Tjin Tham Sjin RM,Satchi-Fainaro R,Birsner AE,Ramanujam VM,Folkman J,Javaherian K

doi

10.1158/0008-5472.CAN-04-1833

subject

Has Abstract

pub_date

2005-05-01 00:00:00

pages

3656-63

issue

9

eissn

0008-5472

issn

1538-7445

pii

65/9/3656

journal_volume

65

pub_type

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