TY - JOUR
T1 - A low-molecular-weight inhibitor against the chemokine receptor CXCR4
T2 - A strong anti-HIV peptide T140
AU - Tamamura, Hirokazu
AU - Xu, Younong
AU - Hattori, Toshio
AU - Zhang, Xiaoyan
AU - Arakaki, Rieko
AU - Kanbara, Kenji
AU - Omagari, Akane
AU - Otaka, Akira
AU - Ibuka, Toshiro
AU - Yamamoto, Naoki
AU - Nakashima, Hideki
AU - Fujii, Nobutaka
N1 - Funding Information:
We thank Dr. D. R. Littman, Skirball Institute for BioMolecular Medicine, New York University Medical Center, for providing pNL-Luc-E-R-vector, 89.6 Env-expressing plasmids and U87.CD4. CXCR4(or CCR5) cells, and Dr. J. A. Hoxie, Hematology-Oncology Division, University of Pennsylvania, for providing the 12G5 antibody through NIH AIDS Research and Reference Reagent Program. Our thanks are also extended to Dr. K. Mochizuki, Faculty of Science and Graduate School of Integrated Science, Yokohama City University, for the synthesis of AMD3100. This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
PY - 1998/12/30
Y1 - 1998/12/30
N2 - T22 ([Tyr(5,l2), Lys7]-polyphemusin II) is an 18-residue peptide amide, which has strong anti-HIV activity. T22 inhibits the T cell line-tropic (T-tropic) HIV-1 infection through its specific binding to a chemokine receptor CXCR4, which serves as a coreceptor for the entry of T-tropic HIV-1 strains. Herein, we report our finding of novel 14-residue CXCR4 inhibitors, T134 and T140, on the basis of the T22 structure. In the assays we examined, T140 showed the highest inhibitory activity against HIV-1 entry and the strongest inhibitory effect on the binding of an anti-CXCR4 monoclonal antibody (12G5) to CXCR4 among all the CXCR4 inhibitors that have been reported up to now.
AB - T22 ([Tyr(5,l2), Lys7]-polyphemusin II) is an 18-residue peptide amide, which has strong anti-HIV activity. T22 inhibits the T cell line-tropic (T-tropic) HIV-1 infection through its specific binding to a chemokine receptor CXCR4, which serves as a coreceptor for the entry of T-tropic HIV-1 strains. Herein, we report our finding of novel 14-residue CXCR4 inhibitors, T134 and T140, on the basis of the T22 structure. In the assays we examined, T140 showed the highest inhibitory activity against HIV-1 entry and the strongest inhibitory effect on the binding of an anti-CXCR4 monoclonal antibody (12G5) to CXCR4 among all the CXCR4 inhibitors that have been reported up to now.
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U2 - 10.1006/bbrc.1998.9871
DO - 10.1006/bbrc.1998.9871
M3 - Article
C2 - 9918823
AN - SCOPUS:0032583575
VL - 253
SP - 877
EP - 882
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -
