Use of 1h-nmr std, waterlogsy and langmuir monolayer techniques for characterization of drug- zein protein complexes

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Use of 1h-nmr std, waterlogsy and langmuir monolayer techniques for characterization of drug- zein protein complexes

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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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07-24-2013, 04:52 PM

nmrlearner

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Use of 1h-nmr std, waterlogsy and langmuir monolayer techniques for characterization of drug- zein protein complexes

Use of 1h-nmr std, waterlogsy and langmuir monolayer techniques for characterization of drug- zein protein complexes

Publication date: Available online 24 July 2013
Source:European Journal of Pharmaceutics and Biopharmaceutics

Author(s): F.F.O. Sousa , A. Luzardo-Álvarez , J. Blanco-Méndez , F.J. Otero-Espinar , M. Martín-Pastor , I. Sandez Macho

Zein is a protein based natural biopolymer containing a large amount of nonpolar amino acids, which has shown the ability to form aggregates and entrap solutes, such as drugs and amino acids to form stable protein-drug complexes. In this work ?-A isotherm, NMR and Dynamic light scattering were used to detect the formation of protein aggregates and the affinity between zein and two different drugs: tetracycline and indomethacin. An effective interaction of zein and the two drugs was evidenced by means of liquid NMR reinforced by means of changes in the surface pressure by ?-A isotherm. The effective interactions zein/drugs under air/water interface were evidenced as a change in the surface pressure of the ?-A isotherm of zein in the presence of drug solutions. The presence of tetracycline in the subphase decreased the area occupied by the monolayer at the expanded region until pressures of 12 mN/m were the areas became similar, but indomethacin produces an increment of the area in both expanded and collapsed region. The feasible methodology employed, focused in the functionality of the protein-drug interaction, can be very promising in the drug delivery field.
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