Structure-based design, synthesis and evaluation of bioactivity of anti-P-gp peptide mimetic.
- Author:
Jing QI
1
;
Hui PENG
;
Ying-dai GAO
;
Chen XU
;
Zhong-qin LIANG
;
Zhen-lun GU
;
Chun-zheng YANG
Author Information
- Publication Type:Journal Article
- MeSH: ATP-Binding Cassette, Sub-Family B, Member 1; chemistry; immunology; Antibodies, Monoclonal; chemistry; Binding, Competitive; Complementarity Determining Regions; chemistry; Drug Design; Drug Resistance, Multiple; Humans; K562 Cells; Molecular Mimicry; Peptides; chemical synthesis; chemistry; metabolism; Protein Conformation
- From: Acta Pharmaceutica Sinica 2003;38(11):826-830
- CountryChina
- Language:Chinese
-
Abstract:
AIMTo design and evaluate the small peptide mimetic of anti-P-glycoprotein (P-gp) antibody (PHMA02).
METHODSFrom the three dementional structure analysis of computer modeling of PHMA02 CDR loops, a small peptide mimetic was designed and determined by flow cytometry.
RESULTSAnti-P-gp peptide mimetic functionally similar to PHMA02 was developed. The peptide mimetic competitively inhibits PHMA02 binding to P-gp and partially block the P-gp function as a drug efflux pump in K562/A02 cells.
CONCLUSIONSome special conformational properties of CDR loops of antibody might serve as lead structures for develop new biological peptide mimetics. Antibody-structure-based design would develop new drug in the future.
