NMR paper A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

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[NMR paper] A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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02-03-2013, 10:19 AM

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A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

Related Articles A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

J Med Chem. 2013 Jan 30;

Authors: Dal Piaz F, Vassallo A, Temraz A, Cotugno R, Belisario MA, Bifulco G, Chini MG, Pisano C, De Tommasi N, Braca A

Abstract
The potential of Heat Shock Protein 90 (Hsp90) as a therapeutic target for numerous diseases has made the identification and optimization of novel Hsp90 inhibitors an emerging therapeutic strategy. A Surface Plasmon Resonance (SPR) approach was adopted to screen some iridoids for their Hsp90 ? binding capability. Twenty-four iridoid derivatives, including 13 new natural compounds, were isolated from the leaves of Tabebuia argentea and petioles of Catalpa bignonioides. Their structures were elucidated by NMR, ESIMS and chemical methods. By means of a panel of chemical and biological approaches, four iridoids were demonstrated to bind Hsp90 ?. In particular, the dimeric iridoid argenteoside A was shown to efficiently inhibit the chaperone in biochemical and cellular assays. Our results disclose C9-type iridoids as a novel class of Hsp90 inhibitors.

PMID: 23362862 [PubMed - as supplied by publisher]

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