Interaction of the octapeptide angiotensin II with a high-affinity single-chain Fv and with peptides derived from the antibody paratope |
| |
Authors: | Cohen P Laune D Teulon I Combes T Pugnière M Badouaille G Granier C Mani J C Simon D |
| |
Institution: | Department of Immunology/Oncology, Sanofi-Synthelabo, 371 rue du Professeur Blayac, 34184 Montpellier Cedex 4, France. |
| |
Abstract: | The amino-acid sequence of the very high-affinity anti-angiotensin II monoclonal antibody 4D8 was predicted from the nucleotide sequence of the heavy and light chain variable genes. The single-chain variable fragment (scFv) was constructed and expressed in Escherichia coli as a soluble protein and at the surface of the filamentous M13 phage and was compared with the full-length antibody (Ab). The scFv showed the same specificity profile and affinity constant as the intact antibody (5.0x10(10) and 8.0x10(10) M(-1), respectively, by Scatchard analysis). Several peptides from the set of overlapping dodecapeptides covering the variable domains of 4D8 mAb were found to specifically bind biotinylated angiotensin II: peptides from the L1, L2, L3 and H1 regions had the strongest capacity to bind the antigen. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|