Binding of tyrosine kinase inhibitor to epidermal growth factor receptor: surface-enhanced infrared absorption microscopy reveals subtle protein secondary structure variations-Reference-Cited by-同舟云学术

Binding of tyrosine kinase inhibitor to epidermal growth factor receptor: surface-enhanced infrared absorption microscopy reveals subtle protein secondary structure variations

Published:2021 Issue:16 Volume:13 Page:7667-7677
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Zucchiatti Paolo¹²³⁴⁵^ORCID,Birarda Giovanni¹²³^ORCID,Cerea Andrea⁶⁷³^ORCID,Semrau Marta S.¹²³^ORCID,Hubarevich Aliaksandr⁶⁷³^ORCID,Storici Paola¹²³^ORCID,De Angelis Francesco⁶⁷³^ORCID,Toma Andrea⁶⁷³^ORCID,Vaccari Lisa¹²³^ORCID

Affiliation:

1. Elettra Sincrotrone Trieste SCpA

2. Trieste

3. Italy

4. Universtà degli studi di Trieste

5. Dipartimento di Fisica

6. Istituto Italiano di Tecnologia

7. Genova

Abstract

Mid-IR plasmonic device for SEIRA microscopy allowed to reveal the subtle conformational changes associated with the binding of Lapatinin inhibitor to the kinase domain of EGFR receptor, a well-known driver of tumorigenesis in pathological settings.

Funder

European Regional Development Fund

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2021/NR/D0NR09200B

Reference68 articles.

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2. Side-chain flexibility in proteins upon ligand binding

3. Ligand-Induced Conformational Changes: Improved Predictions of Ligand Binding Conformations and Affinities