NDLI: Cystine-knot peptides engineered with specificities for (IIb)ß(3) or (IIb)ß(3) and (v)ß(3) integrins are potent inhibitors of platelet aggregation.

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Cystine-knot peptides engineered with specificities for (IIb)ß(3) or (IIb)ß(3) and (v)ß(3) integrins are potent inhibitors of platelet aggregation.

Reagent validation: an underestimated issue in laboratory practice.

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Cystine-knot peptides engineered with specificities for (IIb)ß(3) or (IIb)ß(3) and (v)ß(3) integrins are potent inhibitors of platelet aggregation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Silverman, Adam P. Kariolis, Mihalis S. Cochran, Jennifer R.
Description	Country affiliation: United States Author Affiliation: Silverman AP ( Department of Bioengineering, Cancer Center, Bio-X Program, Stanford University, Stanford, CA 94305, USA.)
Abstract	A truncated form of the Agouti-related protein (AgRP), a member of the cystine-knot family, has shown promise as a scaffold for engineering novel peptides with new molecular recognition properties. In this study, we replaced a constrained six amino acid loop in AgRP with a nine amino acid loop containing an Arg-Gly-Asp integrin recognition motif, and randomized the neighboring residues to create a library of approximately 20 million AgRP variants. We displayed the AgRP mutants as fusions on the surface of yeast and used high-throughput fluorescence-activated cell sorting (FACS) to isolate peptides that bound specifically to the platelet integrin (IIb)ß(3), a clinically important target for the prevention and treatment of thrombosis. These AgRP peptides had equilibrium dissociation (K(D)) constants for (IIb)ß(3) integrin ranging from 60 to 90 nM, and did not bind to (v)ß(3), (v)ß(5), or (5)ß(1) integrins. Using an alternate library screening strategy, we identified AgRP peptides that bound to both (IIb)ß(3) and (v)ß(3) integrins with K(D) values ranging from 40 to 70 nM and 20 to 30 nM, respectively, and did not bind to (v)ß(5) or (5)ß(1) integrins. Unique consensus sequences were identified within both series of AgRP peptides suggesting alternative molecular recognition events that dictate different integrin binding specificities. In addition, the engineered AgRP peptides prevented platelet aggregation as well as or slightly better than the FDA-approved cyclic peptide eptifibatide. Collectively, these data demonstrate that cystine-knot peptides can be generated with high affinity and specificity to closely-related integrins, and provide insights into molecular interactions between small, structured peptide ligands and their receptors.
File Format	HTM / HTML
ISSN	09523499
Issue Number	1
Volume Number	24
e-ISSN	10991352
Journal	Journal of Molecular Recognition
Language	English
Publisher	Wiley
Publisher Date	2011-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Agouti-related Protein Genetics Pharmacology Blood Platelets Drug Effects Integrins Metabolism Platelet Aggregation Inhibitors Platelet Aggregation Chemistry Amino Acid Sequence Humans K562 Cells Mutant Proteins Peptide Library Pichia Protein Binding Recombinant Proteins Journal Article Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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