Dendrimers as size selective inhibitors to protein–protein binding

Chiba, Fumiko; Hu, Ting‐Chou; Twyman, Lance J.; Wagstaff, Mark

doi:10.1039/b806517a

Cited by 34 publications

(55 citation statements)

References 19 publications

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“…Twyman and coworkers designed polyanionic poly(amidoamine) (PAMAM) dendrimers which bind to Cyt c and -chymotrypsin. 69,70 PAMAM dendrimers have also been shown to bind to human serum albumin in an extensive study by the Giri group. 71 They studied binding constants, NMR ( 1 H, STD and DOSY) and molecular dynamic (MD) simulations of 19 PAMAM dendrimers in order to gain insight into the interactions, looking at differences in core, dendrimer generation and terminal group permitting detailed analyses of the key determinants of protein recognition.…”

Section: Dendrimersmentioning

confidence: 99%

Metal complexes as “protein surface mimetics”

Hewitt

Wilson

2016

Chem. Commun.

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A key challenge in chemical biology is to identify small molecule regulators for every single protein. However, protein surfaces are notoriously difficult to recognise with synthetic molecules, often having large flat surfaces that are poorly matched to traditional small molecules. In the surface mimetic approach, a supramolecular scaffold is used to project recognition groups in such a manner as to make multivalent non-covalent contacts over a large area of protein surface. Metal based supramolecular scaffolds offer unique advantages over conventional organic molecules for protein binding, inlcuding greater steroechemcial and geometrical diversity conferred through the metal centre and the potential for direct assessment of binding properties and even visualisation in cells without recourse to further functionalisation. This feature article will highlight the current state of the art in protein surface recognition using metal complexes as surface mimetics.

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Section: Dendrimersmentioning

confidence: 99%

Metal complexes as “protein surface mimetics”

Hewitt

Wilson

2016

Chem. Commun.

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“…To show that ceMoS 2 , in the absence of NIR irradiation, is otherwise biocompatible, we examined its capability to form non‐denaturing host–guest interactions with α‐chymotrypsin (ChT), a serine protease. Here, ChT was chosen for its broad bio‐sensing applicability and its well documented loading capacity in a wide variety of materials, including gold nanoparticles,22 polymeric micelles,23 dendrimers,24 porphyrins,25 carbon nanotubes,26 and GO 14a. 15 As ChT contains a cationic active site that can complex with anionic materials through electrostatic complementation, its loading can be quantified by monitoring enzymatic inhibition by ceMoS 2 .…”

mentioning

confidence: 99%

Chemically Exfoliated MoS₂ as Near‐Infrared Photothermal Agents

Chou¹,

Kaehr

Kim³

et al. 2013

Angew Chem Int Ed

608

394

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“…Here, ChT was chosen for its broad bio-sensing applicability and its well documented loading capacity in a wide variety of materials, including gold nanoparticles, [22] polymeric micelles, [23] dendrimers, [24] porphyrins, [25] carbon nanotubes, [26] and GO. [14a,15] As ChT contains a cationic active site that can complex with anionic materials through electrostatic complementation, its loading can be quantified by monitoring enzymatic inhibition by ceMoS 2 .…”

mentioning

confidence: 99%