ISSN:
0006-3525
Schlagwort(e):
structure-based design
;
Vascular Cell Adhesion Molecule
;
α4β1
;
integrins
;
epitope transfer
;
peptides
;
receptor
;
antagonists
;
nmr spectroscopy
;
Chemistry
;
Polymer and Materials Science
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Chemie und Pharmazie
Notizen:
Results from protein mutagenesis and x-ray crystallographic studies of the multidomain protein Vascular Cell Adhesion Molecule (VCAM) were used to design cyclic octapeptides that retain the critical structural and binding elements of the epitope of VCAM in the interaction with the integrin α4β1 (VLA-4). Changes in the activities of peptide analogues correlated with the relative activities of protein mutants of VCAM, and predicted the properties of two new mutants that bound α4β1 with improved affinity vs wild type protein. The nmr structures of two peptides revealed a high degree of similarity to the structure of the VCAM binding epitope. These results demonstrate that a compact binding epitope identified via protein structure-function studies may be transferred to a synthetically accessible small peptide with the key structure-activity relationships intact. © 1998 John Wiley & Sons, Inc. Biopoly 47: 265-275, 1998
Zusätzliches Material:
4 Ill.
Materialart:
Digitale Medien
Permalink
