Proteomics

Dataset Information

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Affimer reagents as tools to modulate GPVI-ligand interactions

ABSTRACT: We have isolated Affimers that bind to GPVI and characterized their effect on receptor function. An affimer that binds specifically to dimeric GPVI was identified as a novel tool to detect dimeric GPVI. The binding sites of the different Affimers were mapped using HDX-MS, revealing that they interact with functional regions for regulating collagen binding and dimerization.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD046982 | Pride | 2024-10-01

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Anton_DynamX_230922.DnX Other
GPVI_30sec_new.DnX Other
GPVI_Fc.DnX Other
fbsaca_220726_A_GPVI_01.raw.zip Raw
fbsaca_220726_A_GPVI_03.raw.zip Raw
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Publications

<h4>Abstract</h4>Glycoprotein VI (GPVI) plays a key role in collagen-induced platelet aggregation. Affimers are engineered binding protein alternatives to antibodies. We screened and characterized GPVI-binding Affimers as novel tools to probe GPVI function. Among the positive clones, M17, D22, and D18 bound GPVI with the highest affinities (dissociation constant (KD) in the nanomolar range). These Affimers inhibited GPVI-collagen-related peptide (CRP)-XL/collagen interactions, CRP-XL/collagen-in  ...[more]

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