Pubblicazione scientifica

Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

FILONE TECNOLOGICO	TEMA
trasformazione e commercializzazione

RIASSUNTO

Acid proteins capable of nucleating Ca2+ and displaying aggregation capacity play key roles in the formation of calcium carbonate biominerals. The helix-loop helix EF-hands are the most common Ca2+-binding motifs in proteins. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium. Gad m 1, an Atlantic cod β-parvalbumin isoform, is a monomeric EF-hand protein that acts as a Ca2+ buffer in fish muscle; the neutral and acid apo-forms of this protein can form amyloids. Since Ca2+-nucleating proteins have a propensity to form extended β-strand structures, we wondered whether amyloid assemblies of an EF-hand protein were able to influence calcium carbonate crystallization in vitro. Here, we used the Gad m 1 chain as a model to generate monomeric and amyloid assemblies and to analyze their effect on calcite formation in vitro. We found that only amyloid assemblies alter calcite morphology.

DATA

Data di pubblicazione: 20/03/2018

AUTORI

CASTELLANOS MILAGROS
TORRES-PARDO ALMUDENA
RODRIGUEZ-PEREZ ROSA
GASSET MARIA

ENTE DI AFFERENZA

IMDEA NANOSCIENCE 28049 MADRID SPAIN MILAGROS CASTELLANOS IMDEA ORG
DEPARTAMENTO DE QUIM INORGANICA FACULTAD DE QUIM UNIV COMPLUTENSE 28040 MADRID SPAIN ATORRESP QUIM UCM ES
INST INVESTIGACION HOSPITAL UNIVERSITARIO LA PAZ IDIPAZ 28046 MADRID SPAIN ROSA RODRIGUEZ IDIPAZ ES
INSTITUTO QUIMICA-FISICA ROCASOLANO CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS 28006 MADRID SPAIN

RIVISTA

Biomolecules, 8(1), 13

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