Unfolding IGDQ Peptides for Engineering Motogenic Interfaces

Extracellular matrix (ECM)-mimicking surfaces are pivotal tools in understanding adherent cell physiopathology. In this sense, we have recently reported on a discrete set of ECM-mimicking SAMs, among which only those exposing IGDQ peptide-alkanethiols sustain the adhesion of MDA-MB-231 cells by trig...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 33(2017), 30 vom: 01. Aug., Seite 7512-7528
1. Verfasser: De Leo, Federica (VerfasserIn)
Weitere Verfasser: Marega, Riccardo, Corvaglia, Valentina, Tondo, Rodolfo, Lo Cicero, Matteo, Silvestrini, Simone, Bonifazi, Davide
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Peptides
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520 |a Extracellular matrix (ECM)-mimicking surfaces are pivotal tools in understanding adherent cell physiopathology. In this sense, we have recently reported on a discrete set of ECM-mimicking SAMs, among which only those exposing IGDQ peptide-alkanethiols sustain the adhesion of MDA-MB-231 cells by triggering FAK phosphorylation and peculiarly induce the migration of individual cancer cells on the subcentimeter scale. Starting from the experimentally observed relationship among the SAM composition, organization, and biological response, a systematic computational characterization aided in pinpointing the atomistic details through which specific composition and organization achieve the desired biological responsiveness. Specifically, the solvent, number and type of peptides, and presence or absence of surface fillers were accurately considered, creating representative model SAMs simulated by means of classical molecular dynamics (MD) with a view toward unravelling the experimental evidence, revealing how the conformational and structural features of these substrates dictate the specific motogenic responses. Through complementary experimental and computational investigations, it clearly emerges that there exists a distinct and precise mutual interaction among IGDQ-peptides, the surface fillers, and Au, which controls the structural properties of the ECM-mimicking SAMs and thus their motogenic potential 
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700 1 |a Corvaglia, Valentina  |e verfasserin  |4 aut 
700 1 |a Tondo, Rodolfo  |e verfasserin  |4 aut 
700 1 |a Lo Cicero, Matteo  |e verfasserin  |4 aut 
700 1 |a Silvestrini, Simone  |e verfasserin  |4 aut 
700 1 |a Bonifazi, Davide  |e verfasserin  |4 aut 
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