TABLE 4.

Activity and origin of short endostatin peptide fragments.

Peptide Name	Endostatin Residuesa	Activity compared to wild type, unmodified endostatinb	Origin	Reference
H5	31–140	+14%	C- and N-terminal ends removed from human endostatin.	Cho et al. [146]
A-I	6–49	+24%	Human endostatin protein divided into 4 synthetic peptides.	Cattaneo et al. [150] Chillemi et al. [155]
A-II	50–92	No activity
A-III	93–133	No activity
A-IV	134–178	+16%
mP-1	1–27	+27%	Murine endostatin sequence was used to split the endostatin protein into 8 synthetic peptides with overlapping segments of the sequence.	Becker et al. [151] Tanabe et al. [152]
mP-2	23–47	−59%
mP-3	45–69	−43%
mP-4	67–91	−31%
mP-5	89–113	−55%
mP-6	11–134	+19%
mP-7	135–159	−12%
mP-8	157–184	−48%
ES-1	23–34	−44%	Crystal structure of human endostatin protein was used to divide the sequence into 5 synthetic peptide fragments.	Wickström et al. [153]
ES-2	60–70	+8.7%
ES-3	99–111	−56%
ES-4	127–139	−27%
ES-5	171–183	−56%
mEP	N/A	+55%	27 amino acid endostatin peptide from C-terminal endostatin sequence.	Han et al. [104]
mEP-CA	N/A	No activity	Cysteine residue on mEP is substituted for alanine.
mEP-AC	N/A	No activity	Different cysteine residue from mEP-CA is substituted for alanine in mEP.
mEP-AA	N/A	No activity	Both cysteine residues are substituted with alanine on mEP.

^aThe endostatin residues are numbered from N-terminus to C-terminus in human endostatin,

^bActivity reported when available as percentage change from wild type, unmodified endostatin where a positive value is improvement in activity and a negative value is a reduction in activity