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Peri acid

$64

  • Brand : BIOFRON

  • Catalogue Number : BN-O1151

  • Specification : 98%(HPLC)

  • CAS number : 82-75-7

  • Formula : C10H9NO3S

  • Molecular Weight : 223.25

  • PUBCHEM ID : 6722

  • Volume : 5mg

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Catalogue Number

BN-O1151

Analysis Method

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

223.25

Appearance

Botanical Source

Structure Type

Category

SMILES

C1=CC2=C(C(=C1)N)C(=CC=C2)S(=O)(=O)O

Synonyms

1-naphthylamine-8-sulfonic acid/8-Amino-1-naphthalenesulfonic acid/1-Naphthalenesulfonic acid, 8-amino-/8-Aminonaphthalene-1-sulfonic acid/Peri acid

IUPAC Name

8-aminonaphthalene-1-sulfonic acid

Density

1.5±0.1 g/cm3

Solubility

Flash Point

Boiling Point

Melting Point

>350°C

InChl

InChl Key

CYJJLCDCWVZEDZ-UHFFFAOYSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:82-75-7) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

29425876

Abstract

In this study we conducted serial kinetic studies integrated with computational simulations to judge the inhibitory effect of pyrogallol on α-glucosidase, due to the association between this enzyme and the treatment of type 2 diabetes. As a result, we found that pyrogallol bound to the active site of α-glucosidase, interacting with several key residues, such as ASP68, MET69, TYR71, PHE157, PHE158, PHE177, GLN181, HIS348, ASP349, ASP406, VAL407, ASP408, ARG439, and ARG443, which was predicted by performing a protein-ligand docking simulation. Subsequently, we evaluated the inhibitory effect of pyrogallol on α-glucosidase, and found that it induced a mixed type of inhibition in a reversible and quick-binding manner. The relevant kinetic parameters were evaluated to be: IC50=0.72±0.051mM; Ki=0.37±0.018mM. A tertiary conformational change was synchronized with pyrogallol inhibition and modulation of the shape of the active site was correspondingly observed. Our study provides insight into the functional inhibitory role of pyrogallol, which results from its triple-hydroxyl groups interacting with the active site of α-glucosidase. We suggest that compounds similar to pyrogallol (phenolic hydroxyl compounds) which target the key residues of the active site of α-glucosidase could be potential agents for α-glucosidase inhibition.

KEYWORDS

Inhibition; Pyrogallol; α-Glucosidase.

Title

Inhibitory Effect of Pyrogallol on α-Glucosidase: Integrating Docking Simulations With Inhibition Kinetics

Author

Li Zheng 1, Jinhyuk Lee 2, Li-Mei Yue 1, Gyu Tae Lim 2, Jun-Mo Yang 3, Zhuo-Ming Ye 4, Yong-Doo Park 5

Publish date

2018 Jun;

PMID

17971993

Abstract

The design, synthesis, and characterization of novel cavitand-based hetero-TASPs, TASPs having different peptide sequences within one bundle, are described. Three families of hetero-TASPs were designed: the LG3/LG2 family (different linker lengths), LG3/AG3 family (altering helix hydrophobicity), and the LG3/LG2C family (anti-parallel caviteins). These first generation hetero-TASPs were found to be alpha-helical, stable towards guanidine hydrochloride, and monomeric in solution. The LG3/LG2 caviteins exhibited primarily native-like properties. The remaining hetero-TASP families were found to exhibit less dispersion and broader signals in the amide regions of their (1)H NMR spectra than their respective reference caviteins. The success in the design of the LG3/LG2 hetero-TASPs suggests that subsequent hetero-TASPs may have potential to manifest superior native-like structure compared with homo-TASPs, and refinement of the linker and peptide sequences may accomplish this goal.

Title

The Design, Synthesis, and Characterization of the First Cavitand-Based De Novo Hetero-Template-Assembled Synthetic Proteins (Hetero-TASPs)

Author

Heidi E K Huttunen-Hennelly 1, John C Sherman

Publish date

2007 Nov 21

PMID

12416980

Abstract

A set of peptides derived from the N-terminal domain of the ribosomal protein L9 (NTL9) have been characterized in an effort to define the minimum unit of this domain required to fold and to provide model peptides for the analysis of electrostatic interactions in the unfolded state. NTL9 is a 56-residue alpha-beta protein with a beta1-loop-beta2-alpha1-beta3-alpha2 topology. The beta-sheet together with the first helix comprise a simple example of a common supersecondary motif called the split beta-alpha-beta fold. Peptides corresponding to the beta1-loop-beta2 unit are unstructured even when constrained by an introduced disulfide. The pK(a)s of Asp-8 and Glu-17 in these peptides are slightly lower than the values found for shorter peptides but are considerably higher than the values in NTL9. A 34-residue peptide, which represents the beta1-loop-beta2-alpha1 portion of NTL9, is also unstructured. In contrast, a 39-residue peptide corresponding to the entire split beta-alpha-beta motif is folded and monomeric as judged by near- and far-UV CD, two-dimensional NMR, ANS binding experiments, pK(a) measurements, and analytical ultracentrifugation. The fold is very similar to the structure of this region in the intact protein. Thermal and urea unfolding experiments show that it is cooperatively folded with a DeltaG degrees of unfolding of 1.8-2.0 kcal/mol and a T(m) of 58 degrees C. This peptide represents the first demonstration of the independent folding of an isolated split beta-alpha-beta motif, and is one of only four naturally occurring sequences of fewer than 40 residues that has been shown to fold cooperatively in the absence of disulfides or ligand binding.

Title

Characterization of Large Peptide Fragments Derived From the N-terminal Domain of the Ribosomal Protein L9: Definition of the Minimum Folding Motif and Characterization of Local Electrostatic Interactions

Author

Jia-Cherng Horng 1, Viktor Moroz, Daniel J Rigotti, Robert Fairman, Daniel P Raleigh

Publish date

2002 Nov 12


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