scispace - formally typeset
Journal ArticleDOI

N-Methylated cyclic RGD peptides as highly active and selective alpha(V)beta(3) integrin antagonists.

Reads0
Chats0
TLDR
Cyclo(RGDf-N(Me)V-) (P5) was found to be even more active than L1 and is one of the most active and selective compounds in inhibiting vitronectin binding to the alpha(V)beta(3) integrin.
Abstract
The alpha(V)beta(3) integrin receptor plays an important role in human tumor metastasis and tumor-induced angiogenesis. The in vivo inhibition of this receptor by antibodies or by cyclic peptides containing the RGD sequence may in the future be used to selectively suppress these diseases. Here we investigate the influence of N-methylation of the active and selective alpha(V)beta(3) antagonist cyclo(RGDfV) (L1) on biological activity. Cyclo(RGDf-N(Me)V-) (P5) was found to be even more active than L1 and is one of the most active and selective compounds in inhibiting vitronectin binding to the alpha(V)beta(3) integrin. Its high-resolution, three-dimensional structure in water was determined by NMR techniques, distance geometry calculations, and molecular dynamics calculations, providing more insight into the structure-activity relationship.

read more

Citations
More filters
Journal ArticleDOI

Integrins in cancer: biological implications and therapeutic opportunities

TL;DR: Clinical developments emphasize the need to identify how integrin antagonists influence the tumour and its microenvironment.
Journal ArticleDOI

RGD modified polymers: biomaterials for stimulated cell adhesion and beyond

TL;DR: The impacts of RGD peptide surface density, spatial arrangement as well as integrin affinity and selectivity on cell responses like adhesion and migration are discussed.
Journal ArticleDOI

Erratum: Integrins in cancer: biological implications and therapeutic opportunities

TL;DR: Cilengitide is an inhibitor of both αvβ3 and αv β5 integrins, and it was selected in the laboratory by screening a library of cyclic RGD peptides in a cell-free receptor assay for their capacity to inhibit Integrins αvα3 andαvβ5 but not αΙΙbβ3 REF.
Journal ArticleDOI

Crystal Structure of the Extracellular Segment of Integrin αVβ3 in Complex with an Arg-Gly-Asp Ligand

TL;DR: The crystal structure of the extracellular segment of integrin αVβ3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence is reported and ligand binding induces small changes in the orientation of αV relative to β3.
Journal ArticleDOI

Global Conformational Rearrangements in Integrin Extracellular Domains in Outside-In and Inside-Out Signaling

TL;DR: It is shown that a highly bent integrin conformation is physiological and has low affinity for biological ligands.
References
More filters
Journal ArticleDOI

Investigation of exchange processes by two‐dimensional NMR spectroscopy

TL;DR: In this paper, a general technique for the investigation of exchange processes in molecular systems is proposed and demonstrated and applications include the study of chemical exchange, of magnetization transfer by inter-and intramolecular relaxation in liquids, and of spin diffusion and cross-relaxation processes in solids.
Journal ArticleDOI

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions.

TL;DR: A novel approach to tailored selective excitation for the measurement of NMR spectra in non-deuterated aqueous solutions, which effectively combines one selective 180° radiofrequency pulse and two field gradient pulses, achieves highly selective and effective water suppression.
Journal ArticleDOI

Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels

TL;DR: In this article, a single intravascular injection of a cyclic peptide or monoclonal antibody antagonist of integrin alpha v beta 3 disrupts ongoing angiogenesis on the chick chorioallantoic membrane (CAM).
Journal ArticleDOI

1H, 13C and 15N chemical shift referencing in biomolecular NMR

TL;DR: In this paper, a considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules and the authors explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H and 13C chemical shift standards, now used in biomolecular NMR, to those proposed here.
Related Papers (5)