Isolation of a novel basic FGF-binding peptide with potent antiangiogenetic activity.
Isolation of a novel basic FGF-binding peptide with potent antiangiogenetic activity.
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DOI:
10.1111/j.1582-4934.2008.00506.x
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发表时间:
2010-01
影响因子:
5.3
通讯作者:
Li X
中科院分区:
文献类型:
--
作者:
Wu X;Yan Q;Huang Y;Huang H;Su Z;Xiao J;Zeng Y;Wang Y;Nie C;Yang Y;Li X
Basic fibroblast growth factor (bFGF), which plays an important role in tumour angiogenesis and progression, provides a potential target for cancer therapy. Here we screened a phage display heptapeptide library with bFGF and identified 11 specific bFGF-binding phage clones. Two of these clones had identical sequence and the corresponding peptide (referred to as P7) showed high homology to the immunoglobulin-like (Ig-like) domain III (D3) of high-affinity bFGF receptors, FGFR1 (IIIc) and FGFR2 (IIIc). The P7 peptide and its corresponding motif in D3 of FGFRs both carried negative charges and shared similar hydrophobic profiles. Functional analysis demonstrated that synthetic P7 peptides mediate strong inhibition of bFGF-induced cell proliferation and neovascularization. Our results demonstrate that the P7 peptide is a potent bFGF antagonist with strong antiangiogenetic activity, and might have therapeutic potential in cancer therapy.
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影响因子:
6.2
作者:
Luo, Jia;Zhang, Qundan;Zhao, Rui
通讯作者:
Zhao, Rui
影响因子:
1.2
作者:
Tsunenari, I;Yamate, J;Sakuma, S
通讯作者:
Sakuma, S
DOI:
10.1073/pnas.90.22.10643
发表时间:
1993-11-15
影响因子:
11.1
作者:
YAYON, A;AVIEZER, D;KATCHALSKIKATZIR, E
通讯作者:
KATCHALSKIKATZIR, E
DOI:
10.1073/pnas.0436500100
发表时间:
2003-03-04
影响因子:
11.1
作者:
Yeh, BK;Igarashi, M;Mohammadi, M
通讯作者:
Mohammadi, M
影响因子:
3.9
作者:
FASSINA, G;CASSANI, G;ISETTA, AM
通讯作者:
ISETTA, AM